PNAS: Learn row alien bacteria to develop new antibiotics

Massachusetts State University biochemist Peter Chien with the University of California, Berkeley research team by regulating protein degradation to specific destruction of key proteins, in order to rebuild the strict control of bacterial growth and division of the process itself. The study results on September 2, published online in the United States National Academy of Sciences (PNAS).
All organisms using specific enzymes to selectively degrade the specific protein to alter the behavior of cells in vivo or in vitro in response to stimulation signal to the body's growth and react on the ever-changing environment. Energy-dependent protease is considered to be small at the molecular level of the machine, are present in all living organisms, but especially important in bacteria. When the situation has deteriorated, such as bacteria are antibiotic attack, energy-dependent protease precisely the point in time in the process of cell division and destruction of key proteins alternative splicing, cells stop dividing and instead committed to self-repair, spend difficulties. Thus, regulating protein degradation for bacterial virulence and disseminated is critical to understand how bacteria use energy-dependent protease in cellular and molecular level to help find a cure for infectious diseases drugs.

Cell cycle C. crescentus CtrA by activation of transcription factors required for degradation to control, but it is exactly how it works at the molecular level is still unknown. Researchers as early as 20 years ago have learned very important for protein degradation energy-dependent protease ClpXP. ClpXP usually in the cell cycle of the bacteria occur, but not always degrade CtrA, which implies the existence of a more complex regulatory mechanism. CUSABIO HUMAN ATGA ELISA KIT http://www.cusabio.com/ELISA_Kit-114554/ service measured qualitatively and quantitatively. The researchers found that the process of establishing a connection was CtrA ClpXP protease substrates and required a second messenger (help of different cell passages communicate with each other small molecule protein), and is fixed CtrA dephosphorylated adapter protein fixed ClpXP. Researchers three proteins as more than one component aptamers function together to simulate CtrA degradation in crescentus bacteria. The aptamer function only when one of the components of CpdR dephosphorylation and the other ingredients PopA link in the signaling molecule cyclic adenosine two birds (cyclic diguanylate) on. This ensures CtrA only during certain times of degradation of the bacterial cell division cycle.

Chien's research team in the future will be dedicated to finding possible as the active inhibition of bacterial virulence or prevent bacterial antibiotic against environmental pressures targeting new pathways.