It is known to all that the way in which cells convert food into energy is so common among all living things. It puzzled scientists for a long time. Now scientists have discovered a likely reason why the way is shared so widely.
Researchers digested simple sugars such as glucose in a series of chemical reaction to examine how cells make energy from food. The process is almost the same for every kind of cell, including animals, plants and bacteria.
Their news study shows that this process is the most effective way to extract energy. Cells that have more energy can grow and renew faster, giving them and the organism to which they belong an evolutionary advantage.
Scientists at the University of Edinburgh built some complex models to better understand why cells develop the pathways they use to convert sugar into energy. They compared the models in animals and plants with alternative mechanisms that might have evolved instead. They conducted a detailed search for all possible alternatives to the established biological mechanisms known to have existed for billions of years. The results show that the metabolic systems have evolved because they enable cells to produce more energy, compared with alternative pathways.
The key mechanisms that underpin metabolism are found in almost all plants and animals and control the productivity of life on Earth. Although we understand little of how the mechanisms came about, this study shows that our metabolic pathway is a highly developed solution to the problem of how to extract energy from our food, According to Dr Bartomiej Waclaw from the University of Edinburgh's School of Physics and Astronomy who took part in the study published in Nature Communications.
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2015年9月29日星期二
Researchers found a mechanism which is critical for the initiation of embryonic development
Biologists from New York University and scientists at the Stowers Institute for Medical Research have just found a mechanism that promotes activation of genes critical for the initiation of embryonic development.
The paper was published in the journal Genome Research. Christine Rushlow, a professor of biology at NYU, and Julia Zeitlinger, a principal investigator at Kansas City's Stowers Institute, are co-authors of the paper. According to them, our genes are activated by regulatory factors that bind to the control regions of genes called "enhancers"—a process necessary to turn them on at the right time during development. Scientists are so interested in how they gain access to the enhancer regions when they are wrapped in proteins that form the chromosome structure.
They find that a protein called Zelda in the fruit fly embryo is responsible for "opening up" the enhancer regions so that other regulatory factors can gain access and bind to them, thus enabling activation of the associated genes. They also find that enhancer regions appear to be inherently "closed". That's to say, they like to be wrapped in proteins, more so than other non-enhancer regions of the genome, and Zelda tackles the regions to open them up.
"It makes sense that enhancers are intrinsically closed because you do not want developmental genes to turn on inadvertently," says Rushlow, part of NYU's Center for Developmental Genetics. "Instead, it is important that they are tightly controlled so they are active only at the right time and right place. Otherwise, tissue and organs could end up in the wrong place or not form at all."
"We suspect that the more these enhancers are intrinsically closed, the better they can be regulated," says Zeitlinger, who is also an assistant professor at the University of Kansas Medical Center. "It may be counterintuitive, but the tight enclosure allows Zelda to open these enhancer regions just enough for other more tissue-specific factors to come in without risking the enhancers becoming active at the wrong time or place."
Zelda allows many different factors to gain access, thus helping them establish the different tissues of the embryo. The results demonstrate the significance of a mechanism that scouts out enhancers across the genome to prime them for later activation by tissue-specific factors. When Zelda was absent, the binding of other factors such as the Dorsal protein, which is important for proper dorsal-ventral (back-belly) patterning of the fly body, was greatly reduced at target enhancers, and instead redistributed to other regions of the genome that are inherently open.
The findings point out a new-found and critical role of this protein.
Read more:http://www.cusabio.com/catalog-13-1.html
The paper was published in the journal Genome Research. Christine Rushlow, a professor of biology at NYU, and Julia Zeitlinger, a principal investigator at Kansas City's Stowers Institute, are co-authors of the paper. According to them, our genes are activated by regulatory factors that bind to the control regions of genes called "enhancers"—a process necessary to turn them on at the right time during development. Scientists are so interested in how they gain access to the enhancer regions when they are wrapped in proteins that form the chromosome structure.
They find that a protein called Zelda in the fruit fly embryo is responsible for "opening up" the enhancer regions so that other regulatory factors can gain access and bind to them, thus enabling activation of the associated genes. They also find that enhancer regions appear to be inherently "closed". That's to say, they like to be wrapped in proteins, more so than other non-enhancer regions of the genome, and Zelda tackles the regions to open them up.
"It makes sense that enhancers are intrinsically closed because you do not want developmental genes to turn on inadvertently," says Rushlow, part of NYU's Center for Developmental Genetics. "Instead, it is important that they are tightly controlled so they are active only at the right time and right place. Otherwise, tissue and organs could end up in the wrong place or not form at all."
"We suspect that the more these enhancers are intrinsically closed, the better they can be regulated," says Zeitlinger, who is also an assistant professor at the University of Kansas Medical Center. "It may be counterintuitive, but the tight enclosure allows Zelda to open these enhancer regions just enough for other more tissue-specific factors to come in without risking the enhancers becoming active at the wrong time or place."
Zelda allows many different factors to gain access, thus helping them establish the different tissues of the embryo. The results demonstrate the significance of a mechanism that scouts out enhancers across the genome to prime them for later activation by tissue-specific factors. When Zelda was absent, the binding of other factors such as the Dorsal protein, which is important for proper dorsal-ventral (back-belly) patterning of the fly body, was greatly reduced at target enhancers, and instead redistributed to other regions of the genome that are inherently open.
The findings point out a new-found and critical role of this protein.
Read more:http://www.cusabio.com/catalog-13-1.html
B12 plays an important role in Photoreceptor Proteins
A group of scientists has discovered and mapped a light-sensing protein that uses vitamin B12 to perform key functions including gene regulation.
The result comes from studying proteins from the bacterium Thermus thermophilus. It involves at least two findings of broad interest.
Firstly, it expands our knowledge of the biological role of vitamin B12, which was already understood to help convert fat into energy, and to be involved in brain formation, but has now been identified as a key part of photoreceptor proteins—the structures that allow organisms to sense and respond to light.
Secondly, the result shows a new mode of gene regulation, in which the light-sensing proteins play a key role. The bacteria have repurposed existing protein structures that use vitamin B12, and put them to work in new ways, according to the scientists' observation.
The paper describes the photoreceptors in three different states - in the dark, bound to DNA, and after being exposed to light. The finding helps the scientists get all the series of structures and understand how it works at each stage. The details can be found in the journal Nature.
There are nine co-authors of this paper including professor Catherine Drennan of chemistry and biology at MIT, graduate students Percival Yang-Ting Chen, Marco Jost, and Gyunghoon Kang of MIT; Jesus Fernandez-Zapata and S. Padmanabhan of the Institute of Physical Chemistry Rocasolano, in Madrid; and Monserrat Elias-Arnanz, Juan Manuel Ortiz-Guerreo, and Maria Carmen Polanco, of the University of Murcia, in Murcia, Spain.
By studying the structures of the photoreceptor proteins in their three states, the scientists developed a more thorough understanding of the structures, and their functions, than they would have by viewing the proteins in just one state.
Microbes benefit from knowing whether they are in light or darkness. The photoreceptors bind to the DNA in the dark, and prevent activity pertaining to the genes of Thermus thermophilus. When light hits the microbes, the photoreceptor structures cleave and "fall apart," as Drennan puts it, and the bacteria start producing carotenoids, which protect the organisms from negative effects of sunlight, such as DNA damage.
The research also suggests that the exact manner in which the photoreceptors bind to the DNA is novel. The structures contain tetramers, four subunits of the protein, of which three are bound to the genetic material.
The finding is believed to have practical application in the future including the engineering of light-directed control of DNA transcription, or the development of controlled interactions between proteins.
Read more:
http://www.cusabio.com/catalog-13-1.html
The result comes from studying proteins from the bacterium Thermus thermophilus. It involves at least two findings of broad interest.
Firstly, it expands our knowledge of the biological role of vitamin B12, which was already understood to help convert fat into energy, and to be involved in brain formation, but has now been identified as a key part of photoreceptor proteins—the structures that allow organisms to sense and respond to light.
Secondly, the result shows a new mode of gene regulation, in which the light-sensing proteins play a key role. The bacteria have repurposed existing protein structures that use vitamin B12, and put them to work in new ways, according to the scientists' observation.
The paper describes the photoreceptors in three different states - in the dark, bound to DNA, and after being exposed to light. The finding helps the scientists get all the series of structures and understand how it works at each stage. The details can be found in the journal Nature.
There are nine co-authors of this paper including professor Catherine Drennan of chemistry and biology at MIT, graduate students Percival Yang-Ting Chen, Marco Jost, and Gyunghoon Kang of MIT; Jesus Fernandez-Zapata and S. Padmanabhan of the Institute of Physical Chemistry Rocasolano, in Madrid; and Monserrat Elias-Arnanz, Juan Manuel Ortiz-Guerreo, and Maria Carmen Polanco, of the University of Murcia, in Murcia, Spain.
By studying the structures of the photoreceptor proteins in their three states, the scientists developed a more thorough understanding of the structures, and their functions, than they would have by viewing the proteins in just one state.
Microbes benefit from knowing whether they are in light or darkness. The photoreceptors bind to the DNA in the dark, and prevent activity pertaining to the genes of Thermus thermophilus. When light hits the microbes, the photoreceptor structures cleave and "fall apart," as Drennan puts it, and the bacteria start producing carotenoids, which protect the organisms from negative effects of sunlight, such as DNA damage.
The research also suggests that the exact manner in which the photoreceptors bind to the DNA is novel. The structures contain tetramers, four subunits of the protein, of which three are bound to the genetic material.
The finding is believed to have practical application in the future including the engineering of light-directed control of DNA transcription, or the development of controlled interactions between proteins.
Read more:
http://www.cusabio.com/catalog-13-1.html
Innovative tool developed to observe interactions between DNA and enzymatic proteins
Scientists from the University of Washington cooperate with biotechnology company Illumina and have created a new tool - the single-molecule picometer-resolution nanopore tweezers, or SPRNT - to directly detect the single-molecule interactions between DNA and enzymatic proteins. This innovative tool provides a new platform to view and record these nanoscale interactions in real time. It provides fast and reliable characterization of the different mechanisms cellular proteins use to bind to DNA strands—information that could shed new light on the atomic-scale interactions within our cells and help design new drug therapies against pathogens by targeting enzymes that interact with DNA.
The new tool is reported on Sept. 28 in Nature Biotechnology. It is believed to be far more sensitive than other single-molecule tools in the market, for it can really pick up atomic-scale movements that a protein imparts onto DNA. The tool was developed when they were working on a related project.
The research team has been exploring nanopore technology to read DNA sequences quickly for a long time. They tried out a variety of molecular motors to move DNA through the pore when investigating nanopore sequencing. They discovered that their experimental setup was sensitive enough to observe motions much smaller than the distance between adjacent letters on the DNA. After research, they realized that they could detect minute differences in the position of the DNA in the pore and pick up differences in how the proteins were binding to DNA and moving it through the pore.
The SPRNT is sensitive enough to differentiate between the mechanisms that two cellular proteins use to pass DNA through the nanopore opening. One protein, which normally copies DNA, moves along the DNA one letter at a time as it guides DNA through the pore. The second protein, which normally unwinds DNA, instead takes two steps along each DNA letter, which they could pick up by tracking minute changes in the current, according to the report. The report also shows that these two steps involve sequential chemical processes that the protein uses to walk along DNA.
Through the tool you can see the underlying mechanisms and implications, which help you understand more about how life works and how better drugs can be developed.
Read more:http://www.cusabio.com/catalog-9-1.html
The new tool is reported on Sept. 28 in Nature Biotechnology. It is believed to be far more sensitive than other single-molecule tools in the market, for it can really pick up atomic-scale movements that a protein imparts onto DNA. The tool was developed when they were working on a related project.
The research team has been exploring nanopore technology to read DNA sequences quickly for a long time. They tried out a variety of molecular motors to move DNA through the pore when investigating nanopore sequencing. They discovered that their experimental setup was sensitive enough to observe motions much smaller than the distance between adjacent letters on the DNA. After research, they realized that they could detect minute differences in the position of the DNA in the pore and pick up differences in how the proteins were binding to DNA and moving it through the pore.
The SPRNT is sensitive enough to differentiate between the mechanisms that two cellular proteins use to pass DNA through the nanopore opening. One protein, which normally copies DNA, moves along the DNA one letter at a time as it guides DNA through the pore. The second protein, which normally unwinds DNA, instead takes two steps along each DNA letter, which they could pick up by tracking minute changes in the current, according to the report. The report also shows that these two steps involve sequential chemical processes that the protein uses to walk along DNA.
Through the tool you can see the underlying mechanisms and implications, which help you understand more about how life works and how better drugs can be developed.
Read more:http://www.cusabio.com/catalog-9-1.html
2015年9月28日星期一
What's the link between whales and synthetic blood?
Have you ever been curious about why the whales can dive so deeply in such a long time? It is the ultra-stable properties of the proteins that allow deep-diving whales to remain active while holding their breath for up to two hours. The findings just helped Rice University's Ralph and Dorothy Looney Professor of Biochemistry and Cell Biology and his colleagues finish a significance goal to create lifesaving synthetic blood for human trauma patients.
Olson and colleagues George Phillips, Lucian Smith and Premila Samuel compared the muscle protein myoglobin from humans, whales and other deep-diving mammals in the new study they published in the Journal of Biological Chemistry this week. Myoglobin holds oxygen for ready use inside muscle cells, and the study found that marine mammals have ultra-stable versions of myoglobin that tend not to unfold. It was found that stability was the key for cells to make large amounts of myoglobin, which explains why deep-diving mammals can load their muscle cells with far more myoglobin than humans.
"Whales and other deep-diving marine mammals can pack 10-20 times more myoglobin into their cells than humans can, and that allows them to 'download' oxygen directly into their skeletal muscles and stay active even when they are holding their breath," said Olson. "The reason whale meat is so dark is that it's filled with myoglobin that is capable of holding oxygen. But when the myoglobin is newly made, it does not yet contain heme. We found that the stability of heme-free myoglobin is the key factor that allows cells to produce high amounts of myoglobin."
Olson wants to create a strain of bacteria that can generate massive quantities of another protein that's closely related to myoglobin. In the last 20 years, Olson had been working on a larger, more complex oxygen-carrying protein in blood - hemoglobin. His goal was to create synthetic blood for use in transfusions. So far, hospitals and trauma specialists are relying on donated whole blood. But this kind of blood is often in short supply and only can store in a short time. One of the hopes in Olson's plan is to maximize the hemoglobin that a bacterium can express.
The results shows suggest that protein stability is the key. In the research, the amount of fully active myoglobin expressed was directly and strongly dependent on the stability of the protein before it bound the heme group.
In 2013, Michael Berenbrink from Liverpool University and Kevin Campbell from the University of Manitoba noted that deep-diving mammals expressed large amounts of myoglobin in their muscle tissue. They analyzed the genes and available information for all mammalian myoglobins, including those from deep-diving species and found that the myoglobins from aquatic mammals had large positive surface charges compared with those from land animals. They assumed that the charge differences allowed the aquatic species to pack more myoglobin into their muscle cells.
Scientists later did some tests and compared the stability and cell-free expression level of myoglobins from humans, pigs, goosebeak whales, gray seals, sperm whales, dwarf sperm whales and the three mutants, which had low heme affinity but were 50 times more stable than apomyoglobins from the whales. The results showed that the stability of apoprotein is directly correlated with expression levels.
According to Olson, the results of the study clearly verify the expression-stability correlations that had been anecdotally observed in previous work in both mammalian cells and E. coli.
The findings are so important to the projects on synthetic blood substitutes and determining the toxicity of acellular hemoglobin. It is a big step to in the process of creating lifesaving synthetic blood for human trauma patients.
Read more:http://about.cusabio.com/m-185.html
Olson and colleagues George Phillips, Lucian Smith and Premila Samuel compared the muscle protein myoglobin from humans, whales and other deep-diving mammals in the new study they published in the Journal of Biological Chemistry this week. Myoglobin holds oxygen for ready use inside muscle cells, and the study found that marine mammals have ultra-stable versions of myoglobin that tend not to unfold. It was found that stability was the key for cells to make large amounts of myoglobin, which explains why deep-diving mammals can load their muscle cells with far more myoglobin than humans.
"Whales and other deep-diving marine mammals can pack 10-20 times more myoglobin into their cells than humans can, and that allows them to 'download' oxygen directly into their skeletal muscles and stay active even when they are holding their breath," said Olson. "The reason whale meat is so dark is that it's filled with myoglobin that is capable of holding oxygen. But when the myoglobin is newly made, it does not yet contain heme. We found that the stability of heme-free myoglobin is the key factor that allows cells to produce high amounts of myoglobin."
Olson wants to create a strain of bacteria that can generate massive quantities of another protein that's closely related to myoglobin. In the last 20 years, Olson had been working on a larger, more complex oxygen-carrying protein in blood - hemoglobin. His goal was to create synthetic blood for use in transfusions. So far, hospitals and trauma specialists are relying on donated whole blood. But this kind of blood is often in short supply and only can store in a short time. One of the hopes in Olson's plan is to maximize the hemoglobin that a bacterium can express.
The results shows suggest that protein stability is the key. In the research, the amount of fully active myoglobin expressed was directly and strongly dependent on the stability of the protein before it bound the heme group.
In 2013, Michael Berenbrink from Liverpool University and Kevin Campbell from the University of Manitoba noted that deep-diving mammals expressed large amounts of myoglobin in their muscle tissue. They analyzed the genes and available information for all mammalian myoglobins, including those from deep-diving species and found that the myoglobins from aquatic mammals had large positive surface charges compared with those from land animals. They assumed that the charge differences allowed the aquatic species to pack more myoglobin into their muscle cells.
Scientists later did some tests and compared the stability and cell-free expression level of myoglobins from humans, pigs, goosebeak whales, gray seals, sperm whales, dwarf sperm whales and the three mutants, which had low heme affinity but were 50 times more stable than apomyoglobins from the whales. The results showed that the stability of apoprotein is directly correlated with expression levels.
According to Olson, the results of the study clearly verify the expression-stability correlations that had been anecdotally observed in previous work in both mammalian cells and E. coli.
The findings are so important to the projects on synthetic blood substitutes and determining the toxicity of acellular hemoglobin. It is a big step to in the process of creating lifesaving synthetic blood for human trauma patients.
Read more:http://about.cusabio.com/m-185.html
A protein is identified to save bowel inflammation patients
A group of researchers first demonstrated the role of stomach cancer-associated protein tyrosine phosphatase (SAP)-1 in the pathogenesis and prevention of Crohn's disease, ulcerative colitis, and other inflammatory bowel disorders. The group was led by Prof. MATOZAKI Takashi and Associate Prof. MURATA Yoji at the Kobe University Graduate School of Medicine Division of Molecular and Cellular Signaling
Inflammatory bowel diseases are disorders of unknown etiology that are often characterized by abdominal pain, diarrhea, bloody stool, fever, and weight loss. These diseases include Crohn's disease and ulcerative colitis. These symptoms effect too much on patients' daily life and the patients will be pushed at an elevated risk of mortality. And these patients are more likely to be linked with colorectal cancer.
A lot of studies published recently have demonstrated that intestinal epithelial cells are important in regulating bowel inflammation, but the underlying mechanism remains unknown. Before this, the scientists found that SAP-1 localizes to the microvilli of the brush border in gastrointestinal epithelial cells. The transmembrane-type tyrosine phosphatase SAP-1 has an extracellular domain that protrudes into the intestinal lumen and a cytoplasmic domain that mediates tyrosine dephosphorylation of proteins. They showed that SAP-1 ablation in a mouse model of inflammatory bowel disease resulted in a marked increase in the incidence and severity of bowel inflammation, which suggests that SAP-1 plays a protective role against colitis. What's more, carcinoembryonic antigen-related cell adhesion molecule (CEACAM) 20, an intestinal microvillus-specific membrane protein, was identified as the target of SAP-1 tyrosine dephosphorylation. Suppression of CEACAM20 functions via dephosphorylation contributes to preventing colitis. They believe that their findings will drive the development of drugs that target SAP-1 and CEACAM20 to overcome intractable inflammatory bowel diseases by unlocking the anti-inflammatory mechanism of the intestinal epithelial cells.
The future researches of these scientists will be concentrated on taking advantage of the understanding of SAP-1 and CEACAM20 functions to develop new therapeutics for inflammatory bowel disease.
Read more:http://www.cusabio.com/catalog-9-1.html
Inflammatory bowel diseases are disorders of unknown etiology that are often characterized by abdominal pain, diarrhea, bloody stool, fever, and weight loss. These diseases include Crohn's disease and ulcerative colitis. These symptoms effect too much on patients' daily life and the patients will be pushed at an elevated risk of mortality. And these patients are more likely to be linked with colorectal cancer.
A lot of studies published recently have demonstrated that intestinal epithelial cells are important in regulating bowel inflammation, but the underlying mechanism remains unknown. Before this, the scientists found that SAP-1 localizes to the microvilli of the brush border in gastrointestinal epithelial cells. The transmembrane-type tyrosine phosphatase SAP-1 has an extracellular domain that protrudes into the intestinal lumen and a cytoplasmic domain that mediates tyrosine dephosphorylation of proteins. They showed that SAP-1 ablation in a mouse model of inflammatory bowel disease resulted in a marked increase in the incidence and severity of bowel inflammation, which suggests that SAP-1 plays a protective role against colitis. What's more, carcinoembryonic antigen-related cell adhesion molecule (CEACAM) 20, an intestinal microvillus-specific membrane protein, was identified as the target of SAP-1 tyrosine dephosphorylation. Suppression of CEACAM20 functions via dephosphorylation contributes to preventing colitis. They believe that their findings will drive the development of drugs that target SAP-1 and CEACAM20 to overcome intractable inflammatory bowel diseases by unlocking the anti-inflammatory mechanism of the intestinal epithelial cells.
The future researches of these scientists will be concentrated on taking advantage of the understanding of SAP-1 and CEACAM20 functions to develop new therapeutics for inflammatory bowel disease.
Read more:http://www.cusabio.com/catalog-9-1.html
2015年9月25日星期五
Animals in dark polar winter are not always sleeping
Most of us might think that nothing is happening during dark polar winter - not at all. During three consecutive winters in Kongsfjorden, Svalbard, researchers have sampled the activities of many different species and bring some interesting findings to us. They are published in the Cell Press journal Current Biology on September 24.
Their findings change the way people think of marine ecosystem during the polar night. Scientists had assumed that the dark polar night is a period without any biological activities. However, what hide under darkness is a world of activity, beauty and ecosystem importance.
Jorgen Berge of UiT The Arctic University of Norway and the University Centre in Svalbard did a large-scale survey and ecosystem study of the polar night in one of the Svalbard fjords during three consecutive winters with his group members. They found a system buzzing with biological activity instead of an ecosystem in resting state. They found that the diversity and reproductive activity of some species was actually greater during the dark winter than other seasons.
For example, they found that copepods and other zooplankton were actively reproducing as filter-feeding Iceland scallops kept right on growing. Baited traps with time-lapse cameras revealed an abundant and active community of shallow-water scavengers, including whelks, amphipods, and crabs.
What surprised the researchers most were the seabirds. They were able to find their food in the total darkness, which were unexpected before. Even though there are no information about how they are able to do this and how common it is for seabirds to overwinter at the same latitudes, they just make it.
We can’t simply think the dark polar night is a quiet period when things are not happening at all. On the contrary, the dark polar night is an important period for reproduction in many organisms, and it may be more important than the rest of the year.
Read more:http://www.cusabio.com/catalog-9-1.html
Their findings change the way people think of marine ecosystem during the polar night. Scientists had assumed that the dark polar night is a period without any biological activities. However, what hide under darkness is a world of activity, beauty and ecosystem importance.
Jorgen Berge of UiT The Arctic University of Norway and the University Centre in Svalbard did a large-scale survey and ecosystem study of the polar night in one of the Svalbard fjords during three consecutive winters with his group members. They found a system buzzing with biological activity instead of an ecosystem in resting state. They found that the diversity and reproductive activity of some species was actually greater during the dark winter than other seasons.
For example, they found that copepods and other zooplankton were actively reproducing as filter-feeding Iceland scallops kept right on growing. Baited traps with time-lapse cameras revealed an abundant and active community of shallow-water scavengers, including whelks, amphipods, and crabs.
What surprised the researchers most were the seabirds. They were able to find their food in the total darkness, which were unexpected before. Even though there are no information about how they are able to do this and how common it is for seabirds to overwinter at the same latitudes, they just make it.
We can’t simply think the dark polar night is a quiet period when things are not happening at all. On the contrary, the dark polar night is an important period for reproduction in many organisms, and it may be more important than the rest of the year.
Read more:http://www.cusabio.com/catalog-9-1.html
How can mice recognise close relatives?
You may be curious about why mice can recognise close relatives even some of them have never encountered before. The mystery has been unlocked by researchers from the University of Liverpool.
The researchers published a study in Current Biology demonstrating that a species-specific genetic marker called the major urinary protein (MUP), which is detected through the animal's scent, is used by female house mice to select closely related females as nest partners to help look after their offspring. To their astonishment, another scent-based genetic marker, the vertebrate-wide major histocompatibility complex (MHC), is not involved in kin recognition. It was thought to determine how most animals recognise their relatives before.
It proves that animals, including people, tend to cooperating with close relatives because it increases the odds of the genes that they share with relatives being passed to the next generation.
Female house mice usually select relatives as nest partners regardless of prior familiarity, but the genetic markers involved in this recognition have proven extremely difficult to identify.
"This work extends far beyond any previous attempt to identify the genetic basis of kin recognition in vertebrates and strongly challenges the current assumption that there is a common kin-recognition mechanism 'inbuilt' into the immune physiology of all vertebrates," said Professor Jane Hurst, from the University's Institute of Integrative Biology and lead author of the study.
Te researchers are preparing to investigate if other species have evolved similar genetic markers to recognise their relatives and whether these signals evolve only in species that cooperate with relatives to increase their breeding success.
To understand the importance of social groupings in populations can also have implications for captive breeding programmes and help those animals cooperate better.
Read more:http://www.cusabio.com/catalog-9-1.html
The researchers published a study in Current Biology demonstrating that a species-specific genetic marker called the major urinary protein (MUP), which is detected through the animal's scent, is used by female house mice to select closely related females as nest partners to help look after their offspring. To their astonishment, another scent-based genetic marker, the vertebrate-wide major histocompatibility complex (MHC), is not involved in kin recognition. It was thought to determine how most animals recognise their relatives before.
It proves that animals, including people, tend to cooperating with close relatives because it increases the odds of the genes that they share with relatives being passed to the next generation.
Female house mice usually select relatives as nest partners regardless of prior familiarity, but the genetic markers involved in this recognition have proven extremely difficult to identify.
"This work extends far beyond any previous attempt to identify the genetic basis of kin recognition in vertebrates and strongly challenges the current assumption that there is a common kin-recognition mechanism 'inbuilt' into the immune physiology of all vertebrates," said Professor Jane Hurst, from the University's Institute of Integrative Biology and lead author of the study.
Te researchers are preparing to investigate if other species have evolved similar genetic markers to recognise their relatives and whether these signals evolve only in species that cooperate with relatives to increase their breeding success.
To understand the importance of social groupings in populations can also have implications for captive breeding programmes and help those animals cooperate better.
Read more:http://www.cusabio.com/catalog-9-1.html
2015年9月24日星期四
TEP1 gene can also increase malaria transmission through infected mosquitoes
If you're bitten by an infected mosquito, then malaria, a deadly disease, will be transmitted to you. But you may not know that only female mosquitoes bite. Male mosquitoes feed on sugar but not blood. It is because female mosquitoes need an extra dose of nutrients to produce eggs while males do not. However, it doesn't means male mosquitoes don't matter. New research conducted by researchers from the Max Planck Institute of Infection Biology in Berlin and the CNRS in Strasbourg shows that male mosquitoes are probably more important than what people thought before.
The precondition of a female mosquitoes transmitting malaria is that it has to bite an infected person before. Weeks later it bites a healthy person. Why it is not killed by the deadly disease? Mosquitoes also have an immune system as humans do. So some of the infected female mosquitoes may not transmit the disease because the immune system manage to clear infection. Julien Pompon and Elena Levashina uncovered a new function for a gene known to be important for mosquito resistance to malaria.
The gene, called TEP1, was first identified as an immune gene by Levashina in 2001. It is a major killing factoer in female mosquitoes. Her research group now discovers that TEP1 is also implicated in sperm development in male mosquitoes. The TEP1 was found in mosquitoes testes and research showed that it promotes removal of damaged cells during production of spermatozoa, analogous to how discarding bad fruits helps the growing of healthy ones. Once there was no TEP1, male fertility rates were also decreased. Thus TEP1 is necessary for optimal reproduction. This mechanism is also similar to how the TEP1 can help female mosquitoes to resist malaria.
Although it is absolutely good to figure out what could make mosquitoes reproduce less, there is a tough problem. TEP1 is a variable gene, that is, there are different alleles of it all over the world. Different alleles can be inherited by the mosquito offspring after mating, with one always coming from the mother and another from the father. The group also found that one type of TEP1, the S2 allele, can make male mosquitoes better equipped at removing dead cells during sperm production.
This S2 allele confers susceptibility to malaria. In simple words, the same allele that renders mosquito males more fertile, makes females vulnerable to malaria. It means male mosquitoes that can pass on to their offspring a version of TEP1 that is susceptible to malaria could also be better at reproducing. Here comes the conclusion that TEP1 can increase the rate of malaria transmission.
Read more:http://www.cusabio.com/catalog-9-1.html
The precondition of a female mosquitoes transmitting malaria is that it has to bite an infected person before. Weeks later it bites a healthy person. Why it is not killed by the deadly disease? Mosquitoes also have an immune system as humans do. So some of the infected female mosquitoes may not transmit the disease because the immune system manage to clear infection. Julien Pompon and Elena Levashina uncovered a new function for a gene known to be important for mosquito resistance to malaria.
The gene, called TEP1, was first identified as an immune gene by Levashina in 2001. It is a major killing factoer in female mosquitoes. Her research group now discovers that TEP1 is also implicated in sperm development in male mosquitoes. The TEP1 was found in mosquitoes testes and research showed that it promotes removal of damaged cells during production of spermatozoa, analogous to how discarding bad fruits helps the growing of healthy ones. Once there was no TEP1, male fertility rates were also decreased. Thus TEP1 is necessary for optimal reproduction. This mechanism is also similar to how the TEP1 can help female mosquitoes to resist malaria.
Although it is absolutely good to figure out what could make mosquitoes reproduce less, there is a tough problem. TEP1 is a variable gene, that is, there are different alleles of it all over the world. Different alleles can be inherited by the mosquito offspring after mating, with one always coming from the mother and another from the father. The group also found that one type of TEP1, the S2 allele, can make male mosquitoes better equipped at removing dead cells during sperm production.
This S2 allele confers susceptibility to malaria. In simple words, the same allele that renders mosquito males more fertile, makes females vulnerable to malaria. It means male mosquitoes that can pass on to their offspring a version of TEP1 that is susceptible to malaria could also be better at reproducing. Here comes the conclusion that TEP1 can increase the rate of malaria transmission.
Read more:http://www.cusabio.com/catalog-9-1.html
New identified code helps to explain formation of certain cells
We know that human body is made up of trillions of cells and each cell contains thousands of proteins, which determine how the cell is formed and what functions it will perform. Proteins are made up of hundreds of amino acids. The blueprint for each protein is specified by genetic codons, which are triplets of nucleotides that can make 20 different types of amino acids. How amino acids are linked together determines which proteins which proteins are produced, and then what functions the cell will have.
UT Southwestern physiologists have found a new code that helps explain which protein should be created to form a particular type of cell. They got the concept that the sequence of the amino acids and the speed of the process in which the amino acids are put together into a functional protein both matter. The new 'code' within the genetic code uncovers an important regulatory process that impacts all biology, according to Dr. Yi Liu, Professor of Physiology.
Almost every amino acid can be encoded by multiple synonymous codons and that every organism, from humans to fungi, has a preference for certain codons. It was found that if more frequently used codons, they will speed up the process of producing an amino acid chain, while less frequently produced codons slow the process. The use of codons seems to have speed signs on the protein production. That's to say, some segments need to be made fast and others need to be slow.
"The genetic code of nucleic acids is central to life, as it specifies the amino acid sequences of proteins," said Dr. Liu, the Louise W. Kahn Scholar in Biomedical Research. "By influencing the speed with which a protein is assembled from amino acid building blocks, the use of "fast" and "slow" codons can affect protein folding, which is the process that allows a protein to form the right shape to perform a specific function. This speed control mechanism makes sure that proteins are assembled and folded properly in different cells. Therefore, the genetic code not only specifies the sequence of amino acids but also the shape of the protein."
The researchers also found that proteins with identical amino acid sequences will have different functions if they are assembled at different speeds. This is of great importance to identify human disease-causing mutations, for they think a mutation doesn't have to change amnio acid identity to cause a disease.
The study was published in the journal Molecular Cell as the cover story. You can get more detail information there.
Read more:http://about.cusabio.com/m-170.html
UT Southwestern physiologists have found a new code that helps explain which protein should be created to form a particular type of cell. They got the concept that the sequence of the amino acids and the speed of the process in which the amino acids are put together into a functional protein both matter. The new 'code' within the genetic code uncovers an important regulatory process that impacts all biology, according to Dr. Yi Liu, Professor of Physiology.
Almost every amino acid can be encoded by multiple synonymous codons and that every organism, from humans to fungi, has a preference for certain codons. It was found that if more frequently used codons, they will speed up the process of producing an amino acid chain, while less frequently produced codons slow the process. The use of codons seems to have speed signs on the protein production. That's to say, some segments need to be made fast and others need to be slow.
"The genetic code of nucleic acids is central to life, as it specifies the amino acid sequences of proteins," said Dr. Liu, the Louise W. Kahn Scholar in Biomedical Research. "By influencing the speed with which a protein is assembled from amino acid building blocks, the use of "fast" and "slow" codons can affect protein folding, which is the process that allows a protein to form the right shape to perform a specific function. This speed control mechanism makes sure that proteins are assembled and folded properly in different cells. Therefore, the genetic code not only specifies the sequence of amino acids but also the shape of the protein."
The researchers also found that proteins with identical amino acid sequences will have different functions if they are assembled at different speeds. This is of great importance to identify human disease-causing mutations, for they think a mutation doesn't have to change amnio acid identity to cause a disease.
The study was published in the journal Molecular Cell as the cover story. You can get more detail information there.
Read more:http://about.cusabio.com/m-170.html
2015年9月23日星期三
Strange disease kills millions of American starfish
Recently a large number of American starfish are found dead caused by strange diseases. There is no exaggerated that it may be called catastrophic.
"It's staggering, really, the millions of stars that have died. It is not apocalyptic or extreme to say that," says Drew Harvell, a biologist at Cornell University, describing what is widely regarded as one of the worst marine disease events ever recorded.
The starfish is also called sea stars. Millions of the starfish died in recent years. They had their legs curl up and pull away from their bodies, breaking the animals to pieces before they turn to mush, often in a matter of days. Scientists are struggling to find out the reason.
Once densely packed onto the rocks and on the ocean floor, the key predators are simply missing from some locations, their numbers cut by 95 percent or more.
As early as in 2013, this phenomenon called Sea Star Wasting Syndrome was noticed by rangers in Olympic National Park in Washington state. It has now been documented from California to Alaska, and led to die-off that is bigger and more widely spread than any seen before.
There was a group of researchers published their findings indicating strong evidence that a virus was causing the disease last year. Now researchers are studying why the so much more widespread and deadly. They are considering how warmer water brought by climate change is affecting the virus, starfish and the ecosystem.
"We've had anomalously warm oceans for the last two years. Really, what we would call hot water. It is really the dominant thing to consider," Harvell said.
The problem is urgent to be solved even through it's hard to collect data on a big scale. The sea star is kind of the mascot of the intertidal. We should protect these sea stars, the ocean, the ecosystem, thus protecting ourselves.
Read more:http://about.cusabio.com/m-185.html
AG1 gene plays an important role when rice seeds survive underwater
A gene was identified to help rice seeds to survive when grown underwater. The study was published in the leading scientific journal Nature Plants by A team of scientists from the University of California, Riverside and the International Rice Research Institute (IRRI), the Philippines. The study shows that the gene controls the availability of sugar to a growing seed shoot—especially when under flooded conditions.
"The seed of rice is unusual among crops because it can germinate and grow into a young plant that can capture light energy even when the entire process occurs underwater," said Julia Bailey-Serres, one of the paper's authors and a professor of genetics at UC Riverside. "The gene identified—the AG1 gene—helps in this process by allowing energy reserves that are in the seed to be efficiently moved to the growing shoot. The seed planted underwater grows into a seedling that can escape a shallow flood."
There was a gene called SUB1A discovered previously to enable rice plants to survive complete submergence due to a seasonable flood. But this new gene is opposite of that. Bailey-Serres says that Plants with SUB1A essentially hibernate when they are underwater; a situation where energy reserves are safeguarded.
AG1 creates an 'all or nothing' escape mechanism that tricks the seed into thinking that more sugar should be given to its shoot—the plant part that grows into stems and leaves—so that the seed underwater is able to more quickly grow and reach the surface of the water. The mechanism can work up to a water depth of 10 cm and can get 'activated' as soon as the seed is sown underwater.
This gene is one of a family of 13 genes in rice. Other family members are shown to help to move suger from leaves to the young developing seed in fertilized flowers. The important gene is supposed to tell the cell that it does not have enough sugar—keeping the tap open for more to be moved from the seed to the growing shoot.
AG1 works well on moderate stress conditions. When we combined it with the SUB1A gene in the same genetic backgrounds it worked well, although they have opposing mechanisms. However, in some severe stress conditions, AG1 alone is not sufficient. It needs some additional quantitative trait loci (QTLs) or genes that complement the AG1 mechanism.
There is another question they are faced with - Whether seed can be directly seeded underwater – requiring the escape strategy – can also carry the SUB1A gene for submergence tolerance. There are more to be investigated to find the answer.
Read more:http://www.cusabio.com/catalog-9-1.html
"The seed of rice is unusual among crops because it can germinate and grow into a young plant that can capture light energy even when the entire process occurs underwater," said Julia Bailey-Serres, one of the paper's authors and a professor of genetics at UC Riverside. "The gene identified—the AG1 gene—helps in this process by allowing energy reserves that are in the seed to be efficiently moved to the growing shoot. The seed planted underwater grows into a seedling that can escape a shallow flood."
There was a gene called SUB1A discovered previously to enable rice plants to survive complete submergence due to a seasonable flood. But this new gene is opposite of that. Bailey-Serres says that Plants with SUB1A essentially hibernate when they are underwater; a situation where energy reserves are safeguarded.
AG1 creates an 'all or nothing' escape mechanism that tricks the seed into thinking that more sugar should be given to its shoot—the plant part that grows into stems and leaves—so that the seed underwater is able to more quickly grow and reach the surface of the water. The mechanism can work up to a water depth of 10 cm and can get 'activated' as soon as the seed is sown underwater.
This gene is one of a family of 13 genes in rice. Other family members are shown to help to move suger from leaves to the young developing seed in fertilized flowers. The important gene is supposed to tell the cell that it does not have enough sugar—keeping the tap open for more to be moved from the seed to the growing shoot.
AG1 works well on moderate stress conditions. When we combined it with the SUB1A gene in the same genetic backgrounds it worked well, although they have opposing mechanisms. However, in some severe stress conditions, AG1 alone is not sufficient. It needs some additional quantitative trait loci (QTLs) or genes that complement the AG1 mechanism.
There is another question they are faced with - Whether seed can be directly seeded underwater – requiring the escape strategy – can also carry the SUB1A gene for submergence tolerance. There are more to be investigated to find the answer.
Read more:http://www.cusabio.com/catalog-9-1.html
2015年9月22日星期二
A gene which can keep crops healthy under adverse condition has been identified
As you know that plants rely on structures called chloroplasts within their cells to carry out photosynthesis—the process used to capture energy from sunlight by converting carbon dioxide from the air into sugars. During times of stress such as drought, though, the same reaction can also generate substances known as reactive oxygen species, which are toxic to plants and cause them to become damaged or even die.
With the population growth, increasingly shortage of natural resources and the treat of climate change, to develop crops that can survive sub-optimal growing conditions seems Researchers from Oxford University has found a gene that helps plants to remain healthy during times of stress.
According to Professor Paul Jarvis, from the Oxford University's Department of Plant Sciences, the development of chloroplasts is controlled by the presence of a gene known as SP1, which governs the passage of the proteins involved in photosynthesis through the chloroplast's outer membrane. It is suspected that the gene might use this ability to help plants survive in hostile conditions.
The researcher team led by Professor Jarvis wanted to find out if SP1 helped plants to remain healthy by limiting the production of the toxic compounds made during photosynthesis in harsh conditions and has carried out experiments to investigate the idea. Theyworked with three versions of a cress plant known as Arabidopsis thaliana: the naturally occurring wild type, a mutant plant lacking SP1, and an engineered plant that over-expressed SP1. The results indicated that SP1 was responsible for the resilience.
Another set of experiments was carried out to establish how SP1 works at a molecular level. The results demonstrated that SP1 reduces the production of toxic compounds by limiting photosynthesis in times of stress, making plants less likely to suffer serious or fatal damage.
"All plants have the SP1 gene,' explains Professor Jarvis." Now it's just a question of getting plants to over-express it so that they can survive in adverse conditions.'
The researchers are working with more plants to see whether the findings can be used in a wider variety of plants. Hope that the SP1 technology can benefit the improvement of the crop output all around the world.
Read more:http://www.cusabio.com/catalog-9-1.html
With the population growth, increasingly shortage of natural resources and the treat of climate change, to develop crops that can survive sub-optimal growing conditions seems Researchers from Oxford University has found a gene that helps plants to remain healthy during times of stress.
According to Professor Paul Jarvis, from the Oxford University's Department of Plant Sciences, the development of chloroplasts is controlled by the presence of a gene known as SP1, which governs the passage of the proteins involved in photosynthesis through the chloroplast's outer membrane. It is suspected that the gene might use this ability to help plants survive in hostile conditions.
The researcher team led by Professor Jarvis wanted to find out if SP1 helped plants to remain healthy by limiting the production of the toxic compounds made during photosynthesis in harsh conditions and has carried out experiments to investigate the idea. Theyworked with three versions of a cress plant known as Arabidopsis thaliana: the naturally occurring wild type, a mutant plant lacking SP1, and an engineered plant that over-expressed SP1. The results indicated that SP1 was responsible for the resilience.
Another set of experiments was carried out to establish how SP1 works at a molecular level. The results demonstrated that SP1 reduces the production of toxic compounds by limiting photosynthesis in times of stress, making plants less likely to suffer serious or fatal damage.
"All plants have the SP1 gene,' explains Professor Jarvis." Now it's just a question of getting plants to over-express it so that they can survive in adverse conditions.'
The researchers are working with more plants to see whether the findings can be used in a wider variety of plants. Hope that the SP1 technology can benefit the improvement of the crop output all around the world.
Read more:http://www.cusabio.com/catalog-9-1.html
Use customized protein-based sensor to detect viral infection
Biological engineers from MIT have developed a modular system of proteins which can detect a particular DNA sequence in a cell and then give a response like cell death. According to the researchers, the system can be customized to detect any DNA sequence in a mammalian cell and kill cancer cells or cells infected with a virus.
"There is a range of applications for which this could be important," says James Collins, the Termeer Professor of Medical Engineering and Science in MIT's Department of Biological Engineering and Institute of Medical Engineering and Science (IMES). "This allows you to readily design constructs that enable a programmed cell to both detect DNA and act on that detection, with a report system and/or a respond system."
The technology is based on a type of DNA-binding proteins known as zinc fingers. These proteins can be designed to recognize any DNA sequence.
"The technologies are out there to engineer proteins to bind to virtually any DNA sequence that you want," says Shimyn Slomovic, an IMES postdoc and the paper's lead author. "This is used in many ways, but not so much for detection. We felt that there was a lot of potential in harnessing this designable DNA-binding technology for detection."
The researchers needed to link zinc fingers's DNA-binding capability with a consequence-either turning on a fluorescent protein to reveal that the target DNA is present or generating another type of action inside the cell. To create the new system, they exploited a type of protein known as an "intein" and split it into two pieces. The split protein pieces are called "exteins". They only become functional once the intein removes itself while rejoining the two halves.
They decided to divide an intein in two and then attach each portion to a split extein half and a zinc finger protein. The zinc finger proteins are engineered to recognize adjacent DNA sequences within the targeted gene, so if they both find their sequences, the inteins line up and are then cut out, allowing the extein halves to rejoin and form a functional protein. The extein protein is a transcription factor designed to turn on any gene the researchers want.
The researchers also deployed this system to kill cells by linking detection of the DNA target to production of an enzyme called NTR. This enzyme activates a harmless drug precursor called CB 1954, which the researchers added to the petri dish where the cells were growing. When activated by NTR, CB 1954 kills the cells.
There will be more versions in the future which bind to DNA sequences found in cancerous genes and then produce transcription factors that would activate the cells' own programmed cell death pathways. This protein-based sensor can be of great significance.
Read more:http://www.cusabio.com/catalog-13-1.html
"There is a range of applications for which this could be important," says James Collins, the Termeer Professor of Medical Engineering and Science in MIT's Department of Biological Engineering and Institute of Medical Engineering and Science (IMES). "This allows you to readily design constructs that enable a programmed cell to both detect DNA and act on that detection, with a report system and/or a respond system."
The technology is based on a type of DNA-binding proteins known as zinc fingers. These proteins can be designed to recognize any DNA sequence.
"The technologies are out there to engineer proteins to bind to virtually any DNA sequence that you want," says Shimyn Slomovic, an IMES postdoc and the paper's lead author. "This is used in many ways, but not so much for detection. We felt that there was a lot of potential in harnessing this designable DNA-binding technology for detection."
The researchers needed to link zinc fingers's DNA-binding capability with a consequence-either turning on a fluorescent protein to reveal that the target DNA is present or generating another type of action inside the cell. To create the new system, they exploited a type of protein known as an "intein" and split it into two pieces. The split protein pieces are called "exteins". They only become functional once the intein removes itself while rejoining the two halves.
They decided to divide an intein in two and then attach each portion to a split extein half and a zinc finger protein. The zinc finger proteins are engineered to recognize adjacent DNA sequences within the targeted gene, so if they both find their sequences, the inteins line up and are then cut out, allowing the extein halves to rejoin and form a functional protein. The extein protein is a transcription factor designed to turn on any gene the researchers want.
The researchers also deployed this system to kill cells by linking detection of the DNA target to production of an enzyme called NTR. This enzyme activates a harmless drug precursor called CB 1954, which the researchers added to the petri dish where the cells were growing. When activated by NTR, CB 1954 kills the cells.
There will be more versions in the future which bind to DNA sequences found in cancerous genes and then produce transcription factors that would activate the cells' own programmed cell death pathways. This protein-based sensor can be of great significance.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月21日星期一
DNA sequencing device helps to treat UTIs
A new research from the University of East Anglia suggest that a new DNA sequencing device can treat Urinary tract infections (UTIs) more quickly and efficiently. This device is called MinION. It was used to perform nanopore sequencing to characterise bacteria from urine samples four times more quickly than using traditional methods of culturing bacteria.
The method can also detect antibiotic resistance, which improve the efficiency of treatment and stewardship of diminishing antibiotic reserves.
Urinary tract infections are among the most common reasons for prescribing antibiotics. Most are mild and only affect the lower urinary tract, but a few are more troublesome. These 'ascending' UTIs cause a growing burden of hospitalisations, mostly of elderly patients. Infection spills into the bloodstream, leading to a condition called urosepsis, which can be fatal.
Antibiotics are vital, and it must be given urgently especially when bacteria has entered the bloodstream. But unfortunately it takes two days to grow the bacteria in the lab and test which antibiotics kill them.
The research team used a new small DNA sequencing device called Nanopore MinION from Oxford Nanopore Technologies to investigate UTIs quickly - without culturing the bacteria.
The device is about the size of a USB stick. It could detect the bacteria in heavily infected urine and provide its DNA sequence in just 12 hours, which is too much faster than conventional microbiology. This technology is rapid and capable not only of identifying the bacteria in UTIs, but also detecting drug-resistance at the point of clinical need.
There are still more limitations to be overcome. This method currently only works with heavily-infected urine and can't yet predict those resistances that arise by mutation. But as the study is still going on and the technology is developing, more can be achieved.
Read more:http://about.cusabio.com/m-185.html
The method can also detect antibiotic resistance, which improve the efficiency of treatment and stewardship of diminishing antibiotic reserves.
Urinary tract infections are among the most common reasons for prescribing antibiotics. Most are mild and only affect the lower urinary tract, but a few are more troublesome. These 'ascending' UTIs cause a growing burden of hospitalisations, mostly of elderly patients. Infection spills into the bloodstream, leading to a condition called urosepsis, which can be fatal.
Antibiotics are vital, and it must be given urgently especially when bacteria has entered the bloodstream. But unfortunately it takes two days to grow the bacteria in the lab and test which antibiotics kill them.
The research team used a new small DNA sequencing device called Nanopore MinION from Oxford Nanopore Technologies to investigate UTIs quickly - without culturing the bacteria.
The device is about the size of a USB stick. It could detect the bacteria in heavily infected urine and provide its DNA sequence in just 12 hours, which is too much faster than conventional microbiology. This technology is rapid and capable not only of identifying the bacteria in UTIs, but also detecting drug-resistance at the point of clinical need.
There are still more limitations to be overcome. This method currently only works with heavily-infected urine and can't yet predict those resistances that arise by mutation. But as the study is still going on and the technology is developing, more can be achieved.
Read more:http://about.cusabio.com/m-185.html
Evolutionary tree covering 2.3 million species released
Through cooperating whole heartedly of eleven institutions, a first draft of the "tree of life" for about 2.3 million species of animals, plants, fungi and microbes has been released. It depicts the relationships among living things as they diverged from one another over time, tracing back to the beginning of life on Earth more than 3.5 billion years ago.
There are so many smaller trees published over these years, but this is the first time that all of those results are combined into a single tree that covers all of life. It is available online at https://tree.opentreeoflife.org as a digital resource. You can browse, download, use or edit it for free. You can also find it in an article appearing Sept. 18 in the Proceedings of the National Academy of Sciences.
Evolutionary trees are not just for figuring out whether aardvarks are more closely related to moles or manatees, or pinpointing a slime mold's closest cousins, they are also helpful to discover new drugs, increase crop and livestock yields, and trace the origins and spread of infectious diseases and so on.
"As important as showing what we do know about relationships, this first tree of life is also important in revealing what we don't know," said co-author Douglas Soltis of the University of Florida.
The team is also developing software that can enable researchers to log on, update and revise the tree as new data come in for the species remaining to be named or discovered. It is quite important to share data for those works which are already-published or newly-published. Only by sharing can you improve. A few years ago no one was optimistic about the goal of huge trees, but now this Version 1.0. “tree of life” is just online for everyone. It is the starting point.
Read more:http://www.cusabio.com/catalog-9-1.html
There are so many smaller trees published over these years, but this is the first time that all of those results are combined into a single tree that covers all of life. It is available online at https://tree.opentreeoflife.org as a digital resource. You can browse, download, use or edit it for free. You can also find it in an article appearing Sept. 18 in the Proceedings of the National Academy of Sciences.
Evolutionary trees are not just for figuring out whether aardvarks are more closely related to moles or manatees, or pinpointing a slime mold's closest cousins, they are also helpful to discover new drugs, increase crop and livestock yields, and trace the origins and spread of infectious diseases and so on.
"As important as showing what we do know about relationships, this first tree of life is also important in revealing what we don't know," said co-author Douglas Soltis of the University of Florida.
The team is also developing software that can enable researchers to log on, update and revise the tree as new data come in for the species remaining to be named or discovered. It is quite important to share data for those works which are already-published or newly-published. Only by sharing can you improve. A few years ago no one was optimistic about the goal of huge trees, but now this Version 1.0. “tree of life” is just online for everyone. It is the starting point.
Read more:http://www.cusabio.com/catalog-9-1.html
2015年9月18日星期五
Scientists find a mechanism which slows down brain stem cell aging
Recently scientists from the University of Zurich have identified a novel mechanism of how neural stem cells stay relatively free of aging-induced damage. A diffusion barrier regulates the sorting of damaged proteins during cell division. As we know that neural stem cells generate new neurons throughout life in the mammalian brain. But the potential for regeneration in the brain dramatically declines with age. The mechanism just found is of great significance.
Yeast are useful for making wine, bread and brewing beer. At the same time, they are also a good model for neural stem cells in the mammalian brain. It was known that with every division cellular aging factors are asymmetrically distributed between the mother and the daughter cell, allowing for rejuvenation and full life span of the daughter independent of the age of the mother cell. The presence of a diffusion barrier that restricts movement of molecules from one side to the other side of the cell during cell division is partially responsible for that.
To dispose age, Sebastian Jessberger of the Brain Research Institute led a group of scientists to conduct a research and the results showed that also the stem cells of the adult mouse brain asymmetrically segregate aging factors between the mother and the daughter cells. It is a diffusion barrier in the endoplasmic reticulum that is responsible. The barrier keeps the stem cells relatively clean by preventing retention of damaged proteins in the stem cell daughter cell.
Scientists found that the strength of the barrier weakens with advancing age. The weakening leads to reduced asymmetry of damaged protein segregation with increasing age of the stem cell. This is supposed to be a mechanism related to the reduced regeneration capacity in the aged brain for stem cells that retain larger amounts of damaged proteins require longer for the next cell division.
The discovery of the new mechanism is an exciting thing. It is our first step to understand the molecular constituents and the worth of the barrier for stem cell division in the brain. And what remains to be explore is whether the barrier is established in all somatic stem cells of the body.The answer may help finding new way of target age-dependent alterations of stem cell activity in human disease.
Read more:http://www.cusabio.com/catalog-13-1.html
Yeast are useful for making wine, bread and brewing beer. At the same time, they are also a good model for neural stem cells in the mammalian brain. It was known that with every division cellular aging factors are asymmetrically distributed between the mother and the daughter cell, allowing for rejuvenation and full life span of the daughter independent of the age of the mother cell. The presence of a diffusion barrier that restricts movement of molecules from one side to the other side of the cell during cell division is partially responsible for that.
To dispose age, Sebastian Jessberger of the Brain Research Institute led a group of scientists to conduct a research and the results showed that also the stem cells of the adult mouse brain asymmetrically segregate aging factors between the mother and the daughter cells. It is a diffusion barrier in the endoplasmic reticulum that is responsible. The barrier keeps the stem cells relatively clean by preventing retention of damaged proteins in the stem cell daughter cell.
Scientists found that the strength of the barrier weakens with advancing age. The weakening leads to reduced asymmetry of damaged protein segregation with increasing age of the stem cell. This is supposed to be a mechanism related to the reduced regeneration capacity in the aged brain for stem cells that retain larger amounts of damaged proteins require longer for the next cell division.
The discovery of the new mechanism is an exciting thing. It is our first step to understand the molecular constituents and the worth of the barrier for stem cell division in the brain. And what remains to be explore is whether the barrier is established in all somatic stem cells of the body.The answer may help finding new way of target age-dependent alterations of stem cell activity in human disease.
Read more:http://www.cusabio.com/catalog-13-1.html
New butterflies naturally produced by gene transfer been discovered
Research teams from two universities have discovered that genes originating from parasitic wasps are present in the genomes of many butterflies. These genes were acquired through a wasp-associated virus that integrates into DNA. Wasp genes have now been domesticated and likely play a role in in protecting butterflies against other pathogenic viruses.
The study reveals that butterflies constitute naturally produced GMOs (Genetically Modified Organisms) during the course of evolution, including the Monarch, an iconic species for naturalists and well-known for its spectacular migrations. The findings highlight that the genes introduced in GM insects can be transferred between distant species.
Braconid wasps lay their eggs inside caterpillars inject bracovirus to circumvent the caterpillars' immune response to reproduce. The bracoviruses injected can integrate into the DNA of parasitized caterpillars and control caterpillar development to enable them to be the host.
In the genomes of several species of butterfly and moth, including the famous Monarch, the silkworm and insect pests like the Fall Armyworm and the Beet Armyworm, Bracovirus genes can be found. The identified integrated genes are not only remnants. The results suggest that they play a protective role against other viruses present in nature. What's more, the genes harboured by bracoviruses is not limited to viral genes, some of them originated from the wasp. For instance, in armyworm species, a group of genes transferred was more closely related to genes from hymenoptera, including the honey bee, rather than lepidoptera.
The results suggest the risk that GM-parasitoid wasps are produced, as genes artificially introduced into wasp species used for biological control could be transferred into the genomes of the targeted pests. Production of GM wasps expressing insecticide resistance for biological control of pests, may lead to involuntary transmission of this resistance to the herbivorous insects.
The results of the research led by teams from the University of Valencia and the University of Tours were published in PLOS Genetics on the 17th of September 2015. You can get more information about the GM problem.
Read more:http://about.cusabio.com/m-177.html
The study reveals that butterflies constitute naturally produced GMOs (Genetically Modified Organisms) during the course of evolution, including the Monarch, an iconic species for naturalists and well-known for its spectacular migrations. The findings highlight that the genes introduced in GM insects can be transferred between distant species.
Braconid wasps lay their eggs inside caterpillars inject bracovirus to circumvent the caterpillars' immune response to reproduce. The bracoviruses injected can integrate into the DNA of parasitized caterpillars and control caterpillar development to enable them to be the host.
In the genomes of several species of butterfly and moth, including the famous Monarch, the silkworm and insect pests like the Fall Armyworm and the Beet Armyworm, Bracovirus genes can be found. The identified integrated genes are not only remnants. The results suggest that they play a protective role against other viruses present in nature. What's more, the genes harboured by bracoviruses is not limited to viral genes, some of them originated from the wasp. For instance, in armyworm species, a group of genes transferred was more closely related to genes from hymenoptera, including the honey bee, rather than lepidoptera.
The results suggest the risk that GM-parasitoid wasps are produced, as genes artificially introduced into wasp species used for biological control could be transferred into the genomes of the targeted pests. Production of GM wasps expressing insecticide resistance for biological control of pests, may lead to involuntary transmission of this resistance to the herbivorous insects.
The results of the research led by teams from the University of Valencia and the University of Tours were published in PLOS Genetics on the 17th of September 2015. You can get more information about the GM problem.
Read more:http://about.cusabio.com/m-177.html
2015年9月17日星期四
Why bats frequently contact with infectious disease but seldom being infected?
New research concludes that the bat's immune system works in a fundamentally different way from other animals. The research about mastiff bats was conducted by scientists from the Max Planck Institute for Ornithology. It can also help fighting against viral diseases that can be transmitted from animals to humans.
There are very little researches has been conducted about bats'immune system till now. Researchers mentioned above are now trying to bridge this gap. Their findings show the difference between the immune system of bats and other animals. The bats seem to be able to fight off the pathogens without becoming ill themselves. But what makes their immune system so special?
The scientists studied the immune responses of Pallas's mastiff bats (Molossus molossus) in Panama. Those bats live a specific life: during the day they reduce their energy consumption in their roosts in order to save energy. During this period, the bats rest motionless and their body temperature drops. They come to life only at sunset when the mastiff bats set out for the hunt. Then their body temperature rises to more than 40 degrees Celsius as their muscles need to work to keep flying.
However, the high temperature could activate the immune response against pathogens as a type of daily fever. On the contrary, the daily slowdown in their metabolic rate could also inhibit the proliferation of existing pathogens in the body.
The researchers administered a lipopolysaccharide (LPS) to the bats to test the hypothesis. LPS is a compound which is harmless in itself and made up of lipid and sugar components. It is also found on the outer membrane of many pathogens, then the bat's immune system assumes a bacterial attack and switches to defence mode.
However, the daily temperature fluctuations turned out to remain unchanged even after the administration of LPS. The material therefore does not trigger a fever in the bats. What's more, the number of white blood cells in the blood, which is an indicator of the strength of the immune defence, did not increase. But the bats did lose a significant amount of mass within 24 hours meaning that the bats mobilise energy reserves for the immune defence decrease.
The findings indicate that the bats' immune system is switched on but works in a different way. Know more about the difference can help us learn more about the danger of human diseases.
Read more:http://about.cusabio.com/m-190.html
There are very little researches has been conducted about bats'immune system till now. Researchers mentioned above are now trying to bridge this gap. Their findings show the difference between the immune system of bats and other animals. The bats seem to be able to fight off the pathogens without becoming ill themselves. But what makes their immune system so special?
The scientists studied the immune responses of Pallas's mastiff bats (Molossus molossus) in Panama. Those bats live a specific life: during the day they reduce their energy consumption in their roosts in order to save energy. During this period, the bats rest motionless and their body temperature drops. They come to life only at sunset when the mastiff bats set out for the hunt. Then their body temperature rises to more than 40 degrees Celsius as their muscles need to work to keep flying.
However, the high temperature could activate the immune response against pathogens as a type of daily fever. On the contrary, the daily slowdown in their metabolic rate could also inhibit the proliferation of existing pathogens in the body.
The researchers administered a lipopolysaccharide (LPS) to the bats to test the hypothesis. LPS is a compound which is harmless in itself and made up of lipid and sugar components. It is also found on the outer membrane of many pathogens, then the bat's immune system assumes a bacterial attack and switches to defence mode.
However, the daily temperature fluctuations turned out to remain unchanged even after the administration of LPS. The material therefore does not trigger a fever in the bats. What's more, the number of white blood cells in the blood, which is an indicator of the strength of the immune defence, did not increase. But the bats did lose a significant amount of mass within 24 hours meaning that the bats mobilise energy reserves for the immune defence decrease.
The findings indicate that the bats' immune system is switched on but works in a different way. Know more about the difference can help us learn more about the danger of human diseases.
Read more:http://about.cusabio.com/m-190.html
One gene mutation can change entire biological communities
New research have found that one gene mutation in a single species can trigger great changes in whole biological communities.
Scientists from Trinity College Dublin use bacteria to replicate ecological systems in the lab and found that mutations of a single gene that change how one bacterial species interacts with others had huge structural impacts across their multi-species microbial communities. These mutants produce biofilms according to their ability and many of which cause great health problems in body. It had chain effect on other species and completely change the structure of the communities.
"We know that predators are hugely important in influencing how ecosystems are structured, as they control the numbers and diversity of other species in the food web. It is incredible that such a small genetic change can cause these mutants to completely alter communities as much as the extinction of something as important as a predator," said Assistant Professor in Zoology at Trinity, Dr Ian Donohue.
The study shows wide scope for fine-scale genetic differences within populations to change entire ecosystems including microbial ones to lakes, forests and marine system.
"It's amazing to know that just one change in a single gene has the potential to have such a huge effect that it can change whole ecosystems," said Deirdre McClean, lead author of the study and PhD Researcher in Zoology at Trinity.
The results will be helpful to disease researchers, drug developers, ecologists and even geneticists. Besides, better understanding of the effect will be critical to develop treatments aimed at manipulating our gut microbiota specifically.
Read more:http://www.cusabio.com/catalog-10-1.html
Scientists from Trinity College Dublin use bacteria to replicate ecological systems in the lab and found that mutations of a single gene that change how one bacterial species interacts with others had huge structural impacts across their multi-species microbial communities. These mutants produce biofilms according to their ability and many of which cause great health problems in body. It had chain effect on other species and completely change the structure of the communities.
"We know that predators are hugely important in influencing how ecosystems are structured, as they control the numbers and diversity of other species in the food web. It is incredible that such a small genetic change can cause these mutants to completely alter communities as much as the extinction of something as important as a predator," said Assistant Professor in Zoology at Trinity, Dr Ian Donohue.
The study shows wide scope for fine-scale genetic differences within populations to change entire ecosystems including microbial ones to lakes, forests and marine system.
"It's amazing to know that just one change in a single gene has the potential to have such a huge effect that it can change whole ecosystems," said Deirdre McClean, lead author of the study and PhD Researcher in Zoology at Trinity.
The results will be helpful to disease researchers, drug developers, ecologists and even geneticists. Besides, better understanding of the effect will be critical to develop treatments aimed at manipulating our gut microbiota specifically.
Read more:http://www.cusabio.com/catalog-10-1.html
2015年9月15日星期二
New technology developed to unlock DNA secrets of elusive vaquita
The vaquita is one of the most endangered marine mammals on Earth. Protecting these enigmatic animals is extremely urgent. Surprisingly, a new method of teasing information from scarce and highly degraded samples is helping NOAA Fisheries and Mexican scientists unlock the genetic heritage of the endangered Mexican based animal.
Genetic studies can help scientists unlock the DNA secrets of the vaquita. For example, through the study we can get to know the story of how and how long ago the animals evolved into a unique species adapted to warm desert environment when most porpoises live in cool waters. All these information can do great help.
The scientists are faced with a great problem. Fewer than 100 vaquita remain living in the murky waters of the northern Gulf of California. It's hard to find them and collecting samples of their DNA since they are so wary and skittish. Most of the available genetic samples of vaquita come from animals inadvertently killed in fishing nets, which is a chief cause of mortality. They usually have been deteriorated by the time they reach a laboratory.
A small biotechnology company based in Ann Arbor, Michigan, called Enter Swift Biosciences, has developed new methods for dealing with damaged and highly degraded DNA. Traditional methods require sizeable samples of intact DNA in its double-stranded form. The Swife's "next-generation" DNA sample preparation approach can extract genetic material even from bits and pieces of single-stranded DNA which have severely degraded for a long time.
You can obtain useful information though they're not that much. But it is a valuable tools to protect our wildlife resources.
Morin's team then applied the technology to 12 samples of vaquita DNA - including some that were even more degraded and of poorer quality than the harbor porpoise samples. The Swift sample preparation system produced useful data from all of the vaquita samples.
"It was a pleasant surprise to find that we had been able to generate genetic information that had seemed beyond reach without the Swift technologies," said Barbara Taylor, the SWFSC's leading vaquita biologist.
There is not much of a fossil record for porpoises, so genetics also provides the only real way to understand the animal's evolutionary history. Initial findings from the new research now confirm that vaquita apparently split from another species of porpoise from the Southern Hemisphere about 2 to 3 million years ago and have since survived on their own, in relatively small numbers.
The lab plans to apply the technology to other degraded DNA samples to find more evolutionary clues of other animals. The data will be a precious part for preserving endangered animals.
Read more:http://www.cusabio.com/catalog-13-1.html
Genetic studies can help scientists unlock the DNA secrets of the vaquita. For example, through the study we can get to know the story of how and how long ago the animals evolved into a unique species adapted to warm desert environment when most porpoises live in cool waters. All these information can do great help.
The scientists are faced with a great problem. Fewer than 100 vaquita remain living in the murky waters of the northern Gulf of California. It's hard to find them and collecting samples of their DNA since they are so wary and skittish. Most of the available genetic samples of vaquita come from animals inadvertently killed in fishing nets, which is a chief cause of mortality. They usually have been deteriorated by the time they reach a laboratory.
A small biotechnology company based in Ann Arbor, Michigan, called Enter Swift Biosciences, has developed new methods for dealing with damaged and highly degraded DNA. Traditional methods require sizeable samples of intact DNA in its double-stranded form. The Swife's "next-generation" DNA sample preparation approach can extract genetic material even from bits and pieces of single-stranded DNA which have severely degraded for a long time.
You can obtain useful information though they're not that much. But it is a valuable tools to protect our wildlife resources.
Morin's team then applied the technology to 12 samples of vaquita DNA - including some that were even more degraded and of poorer quality than the harbor porpoise samples. The Swift sample preparation system produced useful data from all of the vaquita samples.
"It was a pleasant surprise to find that we had been able to generate genetic information that had seemed beyond reach without the Swift technologies," said Barbara Taylor, the SWFSC's leading vaquita biologist.
There is not much of a fossil record for porpoises, so genetics also provides the only real way to understand the animal's evolutionary history. Initial findings from the new research now confirm that vaquita apparently split from another species of porpoise from the Southern Hemisphere about 2 to 3 million years ago and have since survived on their own, in relatively small numbers.
The lab plans to apply the technology to other degraded DNA samples to find more evolutionary clues of other animals. The data will be a precious part for preserving endangered animals.
Read more:http://www.cusabio.com/catalog-13-1.html
Gene is found in fruit flies to affect fertility of rival males
Pheromones are chemicals cues used for communication for many animals. They are a kind of chemical language guiding important information decisions between animals. Now scientists at the University of Hawai'i - Mānoa's (UHM) Pacific Biosciences Research Center (PBRC) have done a new research identifying a single gene in fruit flies that controls male pheromone production, male fertility and fertility of rival males unexpectedly.
Insects use a wide diversity of pheromone chemical signals to guide their behaviors. But we know little about how the diversity evolves.
"Our work reveals that one way new pheromones are produced is by hijacking genes which are used for other biological processes - in this case, male fertility," said Joanne Yew, assistant professor at PBRC and lead author of the study published today in Nature Communications. "The findings reveal a molecular mechanism by which novel traits evolve, a long-standing problem in evolutionary biology."
The gene is named bond. It uses genetic screening which identified genes in fruit flies that are involved in pheromone synthesis. Researchers used the technique to eliminate the function of other genes within the male reproductive organs one by one. Finally the scientists noted that the male flies in which bond expression was silenced were missing one of the major sex pheromones. The bone they discovered is a powerful gene that encodes an enzyme to make certain pheromones and components of sperm cell membranes, thus affecting behavior and fertility.
The mutant males produced very few offspring compared to normal flies.
One normal male was placed in the company of either mutant males or normal males to determine the influence of bond on social behaviors. A few days later the results showed that, in the absence of the normal chemical signals that signify potential rivals, males lower their sperm investment, which implies that males need a sense of competition to ensure reproductive success.
From the research we can know that fertility is a dynamic trait which can be influenced by social conditions and the perception of sensory signals. What's more, the perception of tastes and smells, that is, the sense that are used to detect pheromones, have great relevance with reproductive physiology and reproductive disorders.
These scientists will research further in this field in the future.
Read more:http://about.cusabio.com/m-171.html
Insects use a wide diversity of pheromone chemical signals to guide their behaviors. But we know little about how the diversity evolves.
"Our work reveals that one way new pheromones are produced is by hijacking genes which are used for other biological processes - in this case, male fertility," said Joanne Yew, assistant professor at PBRC and lead author of the study published today in Nature Communications. "The findings reveal a molecular mechanism by which novel traits evolve, a long-standing problem in evolutionary biology."
The gene is named bond. It uses genetic screening which identified genes in fruit flies that are involved in pheromone synthesis. Researchers used the technique to eliminate the function of other genes within the male reproductive organs one by one. Finally the scientists noted that the male flies in which bond expression was silenced were missing one of the major sex pheromones. The bone they discovered is a powerful gene that encodes an enzyme to make certain pheromones and components of sperm cell membranes, thus affecting behavior and fertility.
The mutant males produced very few offspring compared to normal flies.
One normal male was placed in the company of either mutant males or normal males to determine the influence of bond on social behaviors. A few days later the results showed that, in the absence of the normal chemical signals that signify potential rivals, males lower their sperm investment, which implies that males need a sense of competition to ensure reproductive success.
From the research we can know that fertility is a dynamic trait which can be influenced by social conditions and the perception of sensory signals. What's more, the perception of tastes and smells, that is, the sense that are used to detect pheromones, have great relevance with reproductive physiology and reproductive disorders.
These scientists will research further in this field in the future.
Read more:http://about.cusabio.com/m-171.html
2015年9月14日星期一
A large genome is a good genome
Recently a study shows variation in genome size may be much more important than we throught before. It is obvious that sometimes, a large genome is a good genome. The study was led by researchers at Uppsala University.
"Our study shows that females with larger genome lay more eggs and males with larger genome fertilize more eggs", says research leader G?ran Arnqvist, Professor of Animal Ecology at Uppsala University.
The amount of nuclear DNA per cell, or the size of the genome, varies by orders of magnitude across organisms. We know not too much about the evolutionary forces that are responsible for this variation. the evolutionary forces that are responsible for this variation. For unknown reasons, there are simple plants with a genome almost 50 times as large and grasshoppers with a genome 5 times as large as our own! In fact, the insects with the smallest and largest genomes differ by a factor of 200, yet they all look and act like typical insects.
There are two viewpoints about dramatic differences in biology.
The first suggests that variation in genome size is made up by "junk" DNA that has little bearing on organismal function and that random processes determine genome size.
While the second suggests that the amount of DNA matters and that natural selection shapes genome size. The study of seed beetles now present evidence suggesting that natural selection may be more important.
The study of seed beetles was published in the scientific journal Proceedings of the Royal Society of London. Welcome to read more about the interesting study.
Read more:http://about.cusabio.com/m-187.html
"Our study shows that females with larger genome lay more eggs and males with larger genome fertilize more eggs", says research leader G?ran Arnqvist, Professor of Animal Ecology at Uppsala University.
The amount of nuclear DNA per cell, or the size of the genome, varies by orders of magnitude across organisms. We know not too much about the evolutionary forces that are responsible for this variation. the evolutionary forces that are responsible for this variation. For unknown reasons, there are simple plants with a genome almost 50 times as large and grasshoppers with a genome 5 times as large as our own! In fact, the insects with the smallest and largest genomes differ by a factor of 200, yet they all look and act like typical insects.
There are two viewpoints about dramatic differences in biology.
The first suggests that variation in genome size is made up by "junk" DNA that has little bearing on organismal function and that random processes determine genome size.
While the second suggests that the amount of DNA matters and that natural selection shapes genome size. The study of seed beetles now present evidence suggesting that natural selection may be more important.
The study of seed beetles was published in the scientific journal Proceedings of the Royal Society of London. Welcome to read more about the interesting study.
Read more:http://about.cusabio.com/m-187.html
How do blood cancers develop?
Our immune system always do strange things out of control. For example, when it makes small mistakes, the body amplifies its response to a large extent. It will edit errors in the DNA of developing T and B cells can cause blood cancers.
Recently, researchers from the Perelman School of Medicine, University of Pennsylvania have shown that when the enzyme key to cutting and pasting segments of DNA hits so-called "off-target" spots on a chromosome, the development of immune cells can lead to cancer in animal models. Learning about the nature of these editing errors is quite helpful in designing therapeutic enzymes based on these molecular scissors.
V(D)J recombinase, the editing enzyme that generates specific receptors on the surface of immune cells that match foreign invaders, collectively called antigens, can miss its target from time to time. V(D)J recombinase works only in the early stage of immune cell maturation. In this stage, the diverse array of antibodies and cell-surface receptors found on immune B cells and T cells are respectively made to counteract all the foreign invaders the human body encounters.
Breaks in DNA strands associated with V(D)J cutting are normally repaired with high fidelity by finely tuned molecular machinery. Previous studies from the Roth lab showed that V(D)J recombinase (consisting of the RAG1 and RAG2 proteins) normally sends a break in DNA down the correct repair path by preventing access to other, inappropriate repair mechanisms. This shepherding process can be disabled if the "C" terminus of the RAG2 protein subunit is removed. This causes genomic instability in developing immune cells and, in the absence of a working tumor suppressor protein such as p53, an aggressive form of lymphoma develops in mice.
According to David Roth, the lab of senior author, MD, PhD, chair of the Department of Pathology and Laboratory Medicine, genome wide analysis of lymphomas of the thymus in these mice with the truncated Rag2 protein revealed a surprise: numerous off-target DNA rearrangements, causing deletions. And these rearrangements affected several known and suspected oncogenes and tumor suppressor genes, such as Notch1, Pten, Ikzf1, Jak1, Phlda1, Trat1, and Agpat9.
We can learn more from the genomewide analysis of chromatin marks that normal interactions between the C-terminus of the Rag2 protein subunit and a specific chromatin modification helps maintain the fidelity of DNA target recognition by the enzyme.
It is noteworthy that the cancer-causing effects of off-target deletions mistakenly created by the V(D)J enzyme need to be considered in designing site-specific enzymes for genome modification such as zinc-finger nucleases, TALENS, or CRISPRs.
The Penn team's findings appear online this week in Cell Reports ahead of the print issue. All these foundings contribute much to treatment of blood cancers.
Read more:http://www.cusabio.com/catalog-15-1.html
Recently, researchers from the Perelman School of Medicine, University of Pennsylvania have shown that when the enzyme key to cutting and pasting segments of DNA hits so-called "off-target" spots on a chromosome, the development of immune cells can lead to cancer in animal models. Learning about the nature of these editing errors is quite helpful in designing therapeutic enzymes based on these molecular scissors.
V(D)J recombinase, the editing enzyme that generates specific receptors on the surface of immune cells that match foreign invaders, collectively called antigens, can miss its target from time to time. V(D)J recombinase works only in the early stage of immune cell maturation. In this stage, the diverse array of antibodies and cell-surface receptors found on immune B cells and T cells are respectively made to counteract all the foreign invaders the human body encounters.
Breaks in DNA strands associated with V(D)J cutting are normally repaired with high fidelity by finely tuned molecular machinery. Previous studies from the Roth lab showed that V(D)J recombinase (consisting of the RAG1 and RAG2 proteins) normally sends a break in DNA down the correct repair path by preventing access to other, inappropriate repair mechanisms. This shepherding process can be disabled if the "C" terminus of the RAG2 protein subunit is removed. This causes genomic instability in developing immune cells and, in the absence of a working tumor suppressor protein such as p53, an aggressive form of lymphoma develops in mice.
According to David Roth, the lab of senior author, MD, PhD, chair of the Department of Pathology and Laboratory Medicine, genome wide analysis of lymphomas of the thymus in these mice with the truncated Rag2 protein revealed a surprise: numerous off-target DNA rearrangements, causing deletions. And these rearrangements affected several known and suspected oncogenes and tumor suppressor genes, such as Notch1, Pten, Ikzf1, Jak1, Phlda1, Trat1, and Agpat9.
We can learn more from the genomewide analysis of chromatin marks that normal interactions between the C-terminus of the Rag2 protein subunit and a specific chromatin modification helps maintain the fidelity of DNA target recognition by the enzyme.
It is noteworthy that the cancer-causing effects of off-target deletions mistakenly created by the V(D)J enzyme need to be considered in designing site-specific enzymes for genome modification such as zinc-finger nucleases, TALENS, or CRISPRs.
The Penn team's findings appear online this week in Cell Reports ahead of the print issue. All these foundings contribute much to treatment of blood cancers.
Read more:http://www.cusabio.com/catalog-15-1.html
2015年9月13日星期日
Human relative been found in cave
A new species of human relative was discovered and the big news was announced on 10 September 2015, by the University of the Witwatersrand (Wits University), the National Geographic Society and the Department of Science and Technology (DST) and the National Research Foundation of South Africa (NRF).
The new species is called Homo naledi, which sheds light on the origins and diversity of our genus. Besides, it seems to have intentionally deposited bodies of its dead in a remote cave chamber, a behaviour previously thought limited to humans. It consists of more than 1 550 numbered fossil elements, making the discovery be the largest fossil hominin find yet made on the continent of Africa.
Let's introduce something about h.naledi. It was first found in a cave known as Rising Star in the Cradle of Humankind World Heritage Site, 30 miles) northwest of Johannesburg, South Africa, by Wits University scientists and volunteer cavers. The fossils have yet to be dated. A special team of very slender individuals were set to retrieve them, for those fossils laid about 90 meters from the cave entrance and they can only be accessible through a chute. The team has recovered parts of at least 15 individuals of the same species and a small fraction of the fossils believed to remain in the chamber. Homo naledi is already practically the best-known fossil member of our lineage.
In general, Homo naledi looks like one of the most primitive members of our genus, but it also has some surprisingly human-like features, enough to warrant placing it in the genus Homo, According to John Hawks of the University of Wisconsin-Madison, US, a senior author on the paper describing the new species. H. naledi had a tiny brain, about the size of an average orange (about 500 cubic centimeters), perched atop a very slender body. From the research we can know that on average H. naledi stood approximately 1.5 meters tall and weighed about 45 kilograms.
The findings are published in the scientific journal eLife and reported in the cover story of the October issue of National Geographic magazine and a NOVA/National Geographic Special. If you're interested in the new species of human relative, you can refer to them.
Read more:http://www.cusabio.com/catalog-9-1.html
The new species is called Homo naledi, which sheds light on the origins and diversity of our genus. Besides, it seems to have intentionally deposited bodies of its dead in a remote cave chamber, a behaviour previously thought limited to humans. It consists of more than 1 550 numbered fossil elements, making the discovery be the largest fossil hominin find yet made on the continent of Africa.
Let's introduce something about h.naledi. It was first found in a cave known as Rising Star in the Cradle of Humankind World Heritage Site, 30 miles) northwest of Johannesburg, South Africa, by Wits University scientists and volunteer cavers. The fossils have yet to be dated. A special team of very slender individuals were set to retrieve them, for those fossils laid about 90 meters from the cave entrance and they can only be accessible through a chute. The team has recovered parts of at least 15 individuals of the same species and a small fraction of the fossils believed to remain in the chamber. Homo naledi is already practically the best-known fossil member of our lineage.
In general, Homo naledi looks like one of the most primitive members of our genus, but it also has some surprisingly human-like features, enough to warrant placing it in the genus Homo, According to John Hawks of the University of Wisconsin-Madison, US, a senior author on the paper describing the new species. H. naledi had a tiny brain, about the size of an average orange (about 500 cubic centimeters), perched atop a very slender body. From the research we can know that on average H. naledi stood approximately 1.5 meters tall and weighed about 45 kilograms.
The findings are published in the scientific journal eLife and reported in the cover story of the October issue of National Geographic magazine and a NOVA/National Geographic Special. If you're interested in the new species of human relative, you can refer to them.
Read more:http://www.cusabio.com/catalog-9-1.html
2015年9月10日星期四
A new technology is developed to help scientists understand the work process of proteins and fix the broken proteins. The user-friendly technology is believed to lend a hand to finding new drugs for many diseases, including cancer.
As we know that the human body has a coordinating way of turning its proteins on and off to alter their function and activity in cells. It is phosphorylation, which is the reversible attachment of phosphate groups to proteins. They provide an enormous variety of function and are essential to all forms of life. However, we know little about the detail of this dynamic process.
Researchers have built a cell-free protein synthesis platform technology that can manufacture large quantities of these human phosphoproteins for scientific study using a special strain of E. coli bacteria. The technology can enable scientists to learn more about the function and structure of phosphoproteins and identify the one which are involved in disease. The study was published Sept. 9 by the journal Nature Communications.
Trouble in the phosphorylation process is a trait of disease like cancer, inflammation and Alzheimer's disease. The human proteome is estimated to be phosphorylated at more than 100,000 unique sites. It makes study of phosphorylated proteins and their role in disease be a tough task.
The new technology just developed begins to make the job a tractable problem. It can make these special proteins at unprecedented yields, with a freedom of design that is not possible in living organisms. The consequence of this innovative strategy is enormous in the long run.
Michael C. Jewett is a biochemical engineer who led the Northwestern team. He uses cell-free systems to create new therapies, chemicals and novel materials to impact public health and the environment. Jewett and his colleagues combined state-of-the-art genome engineering tools and engineered biological "parts" into a "plug-and-play" protein expression platform that is cell-free. Cell-free systems activate complex biological systems without using living intact cells. Crude cell lysates, or extracts, are employed instead.
To be specific, the researchers prepared cell lysates of genomically recoded bacteria that incorporate amino acids not found in nature. This allowed them to harness the cell's engineered machinery and turn it into a factory, capable of on-demand biomanufacturing new classes of proteins.
The manufacturing technology will help scientists to unclock the phosphorylation 'code' that exists in the human proteome. The study was published on Sept. 9 by the journal Nature Communications.
Read more:http://about.cusabio.com/m-187.html
As we know that the human body has a coordinating way of turning its proteins on and off to alter their function and activity in cells. It is phosphorylation, which is the reversible attachment of phosphate groups to proteins. They provide an enormous variety of function and are essential to all forms of life. However, we know little about the detail of this dynamic process.
Researchers have built a cell-free protein synthesis platform technology that can manufacture large quantities of these human phosphoproteins for scientific study using a special strain of E. coli bacteria. The technology can enable scientists to learn more about the function and structure of phosphoproteins and identify the one which are involved in disease. The study was published Sept. 9 by the journal Nature Communications.
Trouble in the phosphorylation process is a trait of disease like cancer, inflammation and Alzheimer's disease. The human proteome is estimated to be phosphorylated at more than 100,000 unique sites. It makes study of phosphorylated proteins and their role in disease be a tough task.
The new technology just developed begins to make the job a tractable problem. It can make these special proteins at unprecedented yields, with a freedom of design that is not possible in living organisms. The consequence of this innovative strategy is enormous in the long run.
Michael C. Jewett is a biochemical engineer who led the Northwestern team. He uses cell-free systems to create new therapies, chemicals and novel materials to impact public health and the environment. Jewett and his colleagues combined state-of-the-art genome engineering tools and engineered biological "parts" into a "plug-and-play" protein expression platform that is cell-free. Cell-free systems activate complex biological systems without using living intact cells. Crude cell lysates, or extracts, are employed instead.
To be specific, the researchers prepared cell lysates of genomically recoded bacteria that incorporate amino acids not found in nature. This allowed them to harness the cell's engineered machinery and turn it into a factory, capable of on-demand biomanufacturing new classes of proteins.
The manufacturing technology will help scientists to unclock the phosphorylation 'code' that exists in the human proteome. The study was published on Sept. 9 by the journal Nature Communications.
Read more:http://about.cusabio.com/m-187.html
Monk parakeets stand in pecking order by rank
A study about monk parakeets shows that the places they stand depend on the bird's carefully calibrated perceptions of the rank of their fellow-feathered friends.
Generally, after a week of interactions, which more frequently against those nearby in rank rather than with lower-ranked birds, newly formed groups of monk parakeets quickly perceive rank.
But how do the birds infer rank? It remains to be discovered.
The study published recently in the PLOS Computational Biology indicates how socially complex animal societies evolve and how dominance hierarchies are established.
"Parakeets appear to be able to connect the dots in their groups, remembering chains of aggression, so if A fights B, then watches how B fights C and how C fights D and how D fights E, then A will use this knowledge to adjust how it interacts with E based on all of the fights in between," according to the study's lead author Elizabeth Hobson, a postdoctoral fellow at the National Institute for Mathematical and Biological Synthesis.
In the study, Hobson and co-author Simon DeDeo of Indiana University and the SantaFe Institute analyzed detailed observations of aggression in two independent groups of captive monk parakeets. Each group was observed over the course of 24 days. A total of 1013 wins in one group and 1360 wins in the second group were analyzed.
The complex data shows that as individuals begin to interact and watch the fights of others, they accumulate knowledge of who wins in fights against whom. Once this knowledge is present, the birds use it refine their own behavior, for instance, they focused their aggression by choosing individuals with whom they might be closely matched. You can see that the aggression becomes more strategically directed.
From above we can learn that it's the bird's careful observation of how the other birds interact, which is an act of cognitive complexity, that determines rank amongst these socially precocious birds.
The study allows people to start to understand the interaction between social and cognitive complexity and to begin to compare what we see in the parakeet groups to other socially complex species like primates. That may be of great significance.
Read more:http://about.cusabio.com/m-190.html
Generally, after a week of interactions, which more frequently against those nearby in rank rather than with lower-ranked birds, newly formed groups of monk parakeets quickly perceive rank.
But how do the birds infer rank? It remains to be discovered.
The study published recently in the PLOS Computational Biology indicates how socially complex animal societies evolve and how dominance hierarchies are established.
"Parakeets appear to be able to connect the dots in their groups, remembering chains of aggression, so if A fights B, then watches how B fights C and how C fights D and how D fights E, then A will use this knowledge to adjust how it interacts with E based on all of the fights in between," according to the study's lead author Elizabeth Hobson, a postdoctoral fellow at the National Institute for Mathematical and Biological Synthesis.
In the study, Hobson and co-author Simon DeDeo of Indiana University and the SantaFe Institute analyzed detailed observations of aggression in two independent groups of captive monk parakeets. Each group was observed over the course of 24 days. A total of 1013 wins in one group and 1360 wins in the second group were analyzed.
The complex data shows that as individuals begin to interact and watch the fights of others, they accumulate knowledge of who wins in fights against whom. Once this knowledge is present, the birds use it refine their own behavior, for instance, they focused their aggression by choosing individuals with whom they might be closely matched. You can see that the aggression becomes more strategically directed.
From above we can learn that it's the bird's careful observation of how the other birds interact, which is an act of cognitive complexity, that determines rank amongst these socially precocious birds.
The study allows people to start to understand the interaction between social and cognitive complexity and to begin to compare what we see in the parakeet groups to other socially complex species like primates. That may be of great significance.
Read more:http://about.cusabio.com/m-190.html
2015年9月9日星期三
A protein that plays a central role in maintaining genomic structural stability
We all know that the double-helix shape allows genetic information to be packed into a molecule of human DNA. But how the complex information is packed into the cellular nucleus is still unknown to all. The secret of how this crush of genetic code avoids chaos has been revealed recently. An international team has determined that a protein known as lamin A plays a central role in maintaining genomic structural stability after tracking and analyzing the movement of fluorescently-tagged genomic regions within the nuclei of live cells.
The research group was led by Prof. Yuval Garini of Israel's Bar-Ilan University, and with the participation of members of his lab including Dr. Irena Bronshtein-Berger and Dr. Eldad Kepten, then a PhD candidate. They have shown how this protein is involved in the formation of "cross-links" that limit genetic material's freedom of movement within the nucleus. This creates a stable and linked polymeric structure that promotes chromosomal integrity and makes normal cellular replication possible.
In the study, they explain the biophysical underpinnings of chromosome dynamics and organization and provides biophysical underpinnings of chromosome dynamics and organization.
The mechanism discovered by Garini and his colleagues may have significant implications for the understanding and clinical treatment of disease. What's more, it may pave the way to new approaches toward conditions associated with mutations in the lamin A protein.
Their findings were published on August 24th, 2015 in Nature Communications. If you want to know more about the discovery about the protein-based genome-stabilizing mechanism, you can read more online.
Read more:http://www.cusabio.com/catalog-13-1.html
The research group was led by Prof. Yuval Garini of Israel's Bar-Ilan University, and with the participation of members of his lab including Dr. Irena Bronshtein-Berger and Dr. Eldad Kepten, then a PhD candidate. They have shown how this protein is involved in the formation of "cross-links" that limit genetic material's freedom of movement within the nucleus. This creates a stable and linked polymeric structure that promotes chromosomal integrity and makes normal cellular replication possible.
In the study, they explain the biophysical underpinnings of chromosome dynamics and organization and provides biophysical underpinnings of chromosome dynamics and organization.
The mechanism discovered by Garini and his colleagues may have significant implications for the understanding and clinical treatment of disease. What's more, it may pave the way to new approaches toward conditions associated with mutations in the lamin A protein.
Their findings were published on August 24th, 2015 in Nature Communications. If you want to know more about the discovery about the protein-based genome-stabilizing mechanism, you can read more online.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月8日星期二
Avoid relapse of AML
Researchers have made a small molecule that could deliver a one-two punch to proteins that resist chemotherapy in patients with AML. The researchers are from Rice University, Baylor College of Medicine and the University of Texas MD Anderson Cancer Center. It may be the key to helping patients who are fighting acute myeloid leukemia (AML) avoid a relapse.
The work led by Rice chemist Zachary Ball, Baylor pediatrician Michele Redell and MD Anderson oncologist David Tweardy appears this week in the journal Angewandte Chemie.
The protein STAT3, interferes with chemotherapy by halting the death of cancerous cells and allowing them to proliferate. The molecule locates and attacks a previously unknown binding site on STAT3, thus disrupting its disease-promoting effects.
The STAT3 protein stands for "signal transducer and activator of transcription 3". It is a suspected factor in the relapse of nearly 40 percent of children with AML. The new proximity-driven rhodium(II) catalyst known as MM-206 finds and modifies an inhibitor-binding site on the protein's coiled coil -- literally protein coils coiled around each other -- and delivers the inhibitor, naphthalene sulfonamide, to the modified site.
"We know that increased activity of STAT3 in AML and other cancers helps the cancer cells survive chemotherapy, so any new strategy we can develop to stop that process could mean real benefit for our patients," said Redell, who is also part of the leukemia and lymphoma teams at Texas Children's Hospital.
"Our main advance, from a medicinal perspective, is that this compound also works in a mouse model," Ball said. "All the other compounds worked in cells, but in mice, they weren't potent enough or stable enough."
Follow-up studies should lead to improved versions of the complex. The new discovery is of great importance showing the way to future anti-cancer approaches.
Read more:http://about.cusabio.com/m-171.html
The work led by Rice chemist Zachary Ball, Baylor pediatrician Michele Redell and MD Anderson oncologist David Tweardy appears this week in the journal Angewandte Chemie.
The protein STAT3, interferes with chemotherapy by halting the death of cancerous cells and allowing them to proliferate. The molecule locates and attacks a previously unknown binding site on STAT3, thus disrupting its disease-promoting effects.
The STAT3 protein stands for "signal transducer and activator of transcription 3". It is a suspected factor in the relapse of nearly 40 percent of children with AML. The new proximity-driven rhodium(II) catalyst known as MM-206 finds and modifies an inhibitor-binding site on the protein's coiled coil -- literally protein coils coiled around each other -- and delivers the inhibitor, naphthalene sulfonamide, to the modified site.
"We know that increased activity of STAT3 in AML and other cancers helps the cancer cells survive chemotherapy, so any new strategy we can develop to stop that process could mean real benefit for our patients," said Redell, who is also part of the leukemia and lymphoma teams at Texas Children's Hospital.
"Our main advance, from a medicinal perspective, is that this compound also works in a mouse model," Ball said. "All the other compounds worked in cells, but in mice, they weren't potent enough or stable enough."
Follow-up studies should lead to improved versions of the complex. The new discovery is of great importance showing the way to future anti-cancer approaches.
Read more:http://about.cusabio.com/m-171.html
2015年9月7日星期一
It is proteins that do much of the work in a cell
More than a decade ago scientists found the sequencing of the human genome , and it was undoubtedly considered one of the greatest discoveries in biology. However, it was only the beginning of our in-depth understanding of how cells work. Genes are just blueprints and it is the the proteins, genes' products, that do much of the work in a cell.
A multinational team of scientists have sifted through cells of vastly different organisms, from amoebae to worms to mice to humans, to reveal how proteins fit together to build different cells and bodies.
The wonderful finding is a result of a collaboration between seven research groups from three countries, led by Professor Andrew Emili from the University of Toronto's Donnelly Centre and Professor Edward Marcotte from the University of Texas at Austin. The study uncovered tens of thousands of new protein interactions, accounting for about a quarter of all estimated protein contacts in a cell.
If one of these interactions is lost it can lead to disease, and the map can help scientists spot individual proteins that could be at the root of complex human disorders. Through open access databases, the data will be available to researchers across the world.
Proteins work in teams by sticking to each other to carry out their jobs. Many proteins come together to form so called molecular machines that play key roles, such a building new proteins or recycling those no longer needed by literally grinding them into reusable parts. But when it comes to the vast majority of proteins, for example, there are tens of thousands of them in human cells, we still don't know what they do.
Then Emili and Marcotte's map helps. Using a state-of-the-art method developed by the groups, the researchers were able to fish thousands of protein machineries out of cells and count individual proteins they are made of. They then built a network that, similar to social networks, offers clues into protein function based on which other proteins they hang out with. For example, a new and unstudied protein, whose role we don't yet know, is likely to be involved in fixing damage in a cell if it sticks to cell's known "handymen" proteins
The study gathered information on protein machineries from nine species that represent the tree of life: baker's yeast, sea anemones, amoeba, flies, sea urchins, worms, frogs, mice and humans. The map expands the number of known proteins association over ten fold, and it will trace how they evolved as time goes on.
The researchers discovered that tens of thousands of protein associations remained unchanged since the first ancestral cell appeared, one billion years ago (!), preceding all of animal life on Earth.
The researchers believe that, with tens of thousands of other new protein interactions, the map promises to open many more lines of research into links between proteins and disease, which they are keen to explore in depth over the coming years.
The study comes out in Nature on September 7. Protein assemblies in humans were often identical to those in other species, thus the study will provide the ability to study the genetic basis for a wide variety of diseases and how they present in different species. Hope more secrets can be found.
Read more:http://about.cusabio.com/m-187.html
A multinational team of scientists have sifted through cells of vastly different organisms, from amoebae to worms to mice to humans, to reveal how proteins fit together to build different cells and bodies.
The wonderful finding is a result of a collaboration between seven research groups from three countries, led by Professor Andrew Emili from the University of Toronto's Donnelly Centre and Professor Edward Marcotte from the University of Texas at Austin. The study uncovered tens of thousands of new protein interactions, accounting for about a quarter of all estimated protein contacts in a cell.
If one of these interactions is lost it can lead to disease, and the map can help scientists spot individual proteins that could be at the root of complex human disorders. Through open access databases, the data will be available to researchers across the world.
Proteins work in teams by sticking to each other to carry out their jobs. Many proteins come together to form so called molecular machines that play key roles, such a building new proteins or recycling those no longer needed by literally grinding them into reusable parts. But when it comes to the vast majority of proteins, for example, there are tens of thousands of them in human cells, we still don't know what they do.
Then Emili and Marcotte's map helps. Using a state-of-the-art method developed by the groups, the researchers were able to fish thousands of protein machineries out of cells and count individual proteins they are made of. They then built a network that, similar to social networks, offers clues into protein function based on which other proteins they hang out with. For example, a new and unstudied protein, whose role we don't yet know, is likely to be involved in fixing damage in a cell if it sticks to cell's known "handymen" proteins
The study gathered information on protein machineries from nine species that represent the tree of life: baker's yeast, sea anemones, amoeba, flies, sea urchins, worms, frogs, mice and humans. The map expands the number of known proteins association over ten fold, and it will trace how they evolved as time goes on.
The researchers discovered that tens of thousands of protein associations remained unchanged since the first ancestral cell appeared, one billion years ago (!), preceding all of animal life on Earth.
The researchers believe that, with tens of thousands of other new protein interactions, the map promises to open many more lines of research into links between proteins and disease, which they are keen to explore in depth over the coming years.
The study comes out in Nature on September 7. Protein assemblies in humans were often identical to those in other species, thus the study will provide the ability to study the genetic basis for a wide variety of diseases and how they present in different species. Hope more secrets can be found.
Read more:http://about.cusabio.com/m-187.html
2015年9月6日星期日
Cheaper antivenom is coming
Recently, researchers from six institutions including the University of Copenhagen and the National Aquarium of Denmark (Den Blå Planet) have successfully identified the exact composition of sea snake venom, which makes the future development of synthetic antivenoms more realistic.
At present, sea snake anitvenom costs nearly USD 2000, which is obviously too expensive. The new findings referred to above could result in a future production of synthetic antivenoms for as little as USD 10-100.
In many tropical and subtropical countries, Venomous snakebites becomes a major health concern. There are more than 10 million bites each year. In Sub-Saharan Africa alone, an estimated one million snakebites occur annually and about half of them need treatment, many result in amputations and a significant amount result in deaths.
When people in poor countries are bitten, including working fishermen and children playing in the ocean, they are more likely to be left to die because it is extremely expensive to save them, not because they cannot be saved. More lives can be saved if there are more inexpensive antivenoms produced.
Antivenoms are still produced by traditional animal immunization procedures, which has a number of drawbacks, such as allergic reactions, which in the worst instances end in death. Yet technological advances within biopharmaceuticals and medicinal chemistry could pave the way for rational drug design approaches to snake toxins. This could eliminate the use of animals and bring forward more effective therapies for snakebite envenoming.
Hope more people can benefit from the new findings.
Read more:http://www.cusabio.com/catalog-13-1.html
At present, sea snake anitvenom costs nearly USD 2000, which is obviously too expensive. The new findings referred to above could result in a future production of synthetic antivenoms for as little as USD 10-100.
In many tropical and subtropical countries, Venomous snakebites becomes a major health concern. There are more than 10 million bites each year. In Sub-Saharan Africa alone, an estimated one million snakebites occur annually and about half of them need treatment, many result in amputations and a significant amount result in deaths.
When people in poor countries are bitten, including working fishermen and children playing in the ocean, they are more likely to be left to die because it is extremely expensive to save them, not because they cannot be saved. More lives can be saved if there are more inexpensive antivenoms produced.
Antivenoms are still produced by traditional animal immunization procedures, which has a number of drawbacks, such as allergic reactions, which in the worst instances end in death. Yet technological advances within biopharmaceuticals and medicinal chemistry could pave the way for rational drug design approaches to snake toxins. This could eliminate the use of animals and bring forward more effective therapies for snakebite envenoming.
Hope more people can benefit from the new findings.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月5日星期六
New proteins have been found to save plants facing with high salt problem
Studies before show that high salt in soil dramatically stresses plant biology and reduces the growth and yield of crops. A study led by professor Staffan Persson, from University of Melbourne, Australia, formerly at the Max Planck Institute of Molecular Plant Physiology, found specific proteins that allow plants to grow better under salt stress, and may help breed future generations of more salt-tolerant crop plants.
Humans can move away from the salty snacks or drink more water, but if a plant is stuck in high salt (or saline) soils, it must use other tactics to cope. More and more of the world' crops are facing salt stress with high salt in soils (also known as salinity) affecting 20% of the total, and 33% of irrigated, agricultural lands worldwide. We need to increase production of food by 70% to feed an additional 2.3 billion people by 2050. Salinity is a major limiting factor for this goal as more than 50% of the arable land may be salt afflicted by the year 2050. Thus finding genes and mechanisms that can improve plant growth under such conditions is of utmost urgency.
"Plants need to make bigger cells and more of them if they want to grow and develop, " said Prof Persson.
"Unlike animal cells, plant cells are surrounded by a cellular exoskeleton, called cell walls which direct plant growth and protect the plant against diseases. Importantly, most of the plants biomass is made up of the cell wall with cellulose being the major component.
"Hence, plant growth largely depend on the ability of plants to produce cell walls and cellulose, also under stress conditions, and it is therefore no surprise that research on cell wall biosynthesis is of high priority."
The present study shows that an previously unknown family of proteins supports the cellulose synthase machinery under salt stress conditions, and was named "Companions of Cellulose synthase (CC). These CC proteins are part of the cellulose synthase complex during cellulose synthesis. The researchers found that the CC gene activity was increased when plants were exposed to high salt concentrations.
"In an additional step, we made fluorescent versions of the CC proteins and observed, with the help of a special microscope, where and how they function. It was quite a surprise to see that they were able to maintain the organization of microtubules under salt stress. This function helped the plants to maintain cellulose synthesis during the stress", said Dr. Anne Endler, co-first author of this study.
The research group proved that the plants lacking the CC activity were unable to maintain their microtubules intact. The loss in microtubule function led to a failure in maintaining cellulose synthesis, which explained the reduction in plant growth on salt.
The results of the study provide a mechanism for how the CC proteins aid plant biomass production under salt stress and help plants to grow on salt. The team has identified a protein family that helps plants to grow on salt, and outlined a mechanism for how these proteins aid the plants to produce their biomass under salt stress conditions. The study was published the day before yesterday in the journal Cell.
Read more:http://www.cusabio.com/catalog-13-1.html
Humans can move away from the salty snacks or drink more water, but if a plant is stuck in high salt (or saline) soils, it must use other tactics to cope. More and more of the world' crops are facing salt stress with high salt in soils (also known as salinity) affecting 20% of the total, and 33% of irrigated, agricultural lands worldwide. We need to increase production of food by 70% to feed an additional 2.3 billion people by 2050. Salinity is a major limiting factor for this goal as more than 50% of the arable land may be salt afflicted by the year 2050. Thus finding genes and mechanisms that can improve plant growth under such conditions is of utmost urgency.
"Plants need to make bigger cells and more of them if they want to grow and develop, " said Prof Persson.
"Unlike animal cells, plant cells are surrounded by a cellular exoskeleton, called cell walls which direct plant growth and protect the plant against diseases. Importantly, most of the plants biomass is made up of the cell wall with cellulose being the major component.
"Hence, plant growth largely depend on the ability of plants to produce cell walls and cellulose, also under stress conditions, and it is therefore no surprise that research on cell wall biosynthesis is of high priority."
The present study shows that an previously unknown family of proteins supports the cellulose synthase machinery under salt stress conditions, and was named "Companions of Cellulose synthase (CC). These CC proteins are part of the cellulose synthase complex during cellulose synthesis. The researchers found that the CC gene activity was increased when plants were exposed to high salt concentrations.
"In an additional step, we made fluorescent versions of the CC proteins and observed, with the help of a special microscope, where and how they function. It was quite a surprise to see that they were able to maintain the organization of microtubules under salt stress. This function helped the plants to maintain cellulose synthesis during the stress", said Dr. Anne Endler, co-first author of this study.
The research group proved that the plants lacking the CC activity were unable to maintain their microtubules intact. The loss in microtubule function led to a failure in maintaining cellulose synthesis, which explained the reduction in plant growth on salt.
The results of the study provide a mechanism for how the CC proteins aid plant biomass production under salt stress and help plants to grow on salt. The team has identified a protein family that helps plants to grow on salt, and outlined a mechanism for how these proteins aid the plants to produce their biomass under salt stress conditions. The study was published the day before yesterday in the journal Cell.
Read more:http://www.cusabio.com/catalog-13-1.html
2015年9月2日星期三
DNA origami contributing to building nanodevices
Recent years scientists have been studying ways to use synthetic DNA as a building block to create smaller and faster devices, and they have made great progress in this field. Each DNA strand is formed of one of four "codes" which can link to only one complementary code each, thus binding two DNA strands together. Scientists are using this inherent coding to manipulate and "fold" DNA to form "origami nanostructures": extremely small two- and three-dimensional shapes that can then be used as construction material to build nanodevices such as nanomotors for use in targeted drug delivery inside the body. But assembling DNA origami units into larger structures remains challenging.
A team of scientists at Kyoto University's Institute for Integrated Cell-Material Sciences (iCeMS) has developed an approach that could bring us one step closer to the nanomachines of the future.
They used a double layer of lipids (fats) containing both a positive and a negative charge. DNA origami structures were weakly absorbed onto the lipid layer through an electrostatic interaction. The weak bond between the origami structures and the lipid layer allowed them to move more freely than in other approaches, facilitating their interaction with one another to assemble and form larger structures.
The scientists anticipate that this approach will further expand the potential applications of DNA origami structures and their assemblies in the fields of nanotechnology, biophysics and synthetic biology.
Read more:http://about.cusabio.com/m-179.html
A team of scientists at Kyoto University's Institute for Integrated Cell-Material Sciences (iCeMS) has developed an approach that could bring us one step closer to the nanomachines of the future.
They used a double layer of lipids (fats) containing both a positive and a negative charge. DNA origami structures were weakly absorbed onto the lipid layer through an electrostatic interaction. The weak bond between the origami structures and the lipid layer allowed them to move more freely than in other approaches, facilitating their interaction with one another to assemble and form larger structures.
The scientists anticipate that this approach will further expand the potential applications of DNA origami structures and their assemblies in the fields of nanotechnology, biophysics and synthetic biology.
Read more:http://about.cusabio.com/m-179.html
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