How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. Export

@article{citeulike:2923935, abstract = {The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.}, address = {Microbiologie et G\'{e}n\'{e}tique Mol\'{e}culaire, INRA-CNRS-INA PG UMR 2585, Thiverval-Grignon, France. Josef.Deutscher@grignon.inra.fr}, author = {Deutscher, J. and Francke, C. and Postma, P. W.}, citeulike-article-id = {2923935}, citeulike-linkout-0 = {http://dx.doi.org/10.1128/MMBR.00024-06}, citeulike-linkout-1 = {http://mmbr.asm.org/cgi/content/abstract/70/4/939}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17158705}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17158705}, doi = {10.1128/MMBR.00024-06}, issn = {1092-2172}, journal = {Microbiology and molecular biology reviews : MMBR}, keywords = {background, carbohydrate, general, metabolism, phosphotransferase, phosphotransferase\_system, pts, regulation}, month = {December}, number = {4}, pages = {939--1031}, posted-at = {2008-06-24 16:57:10}, priority = {3}, title = {How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.}, url = {http://dx.doi.org/10.1128/MMBR.00024-06}, volume = {70}, year = {2006} }

TY - JOUR ID - citeulike:2923935 L3 - citeulike-article-id:2923935 N2 - The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens. IS - 4 JF - Microbiology and molecular biology reviews : MMBR SN - 1092-2172 AD - Microbiologie et Génétique Moléculaire, INRA-CNRS-INA PG UMR 2585, Thiverval-Grignon, France. Josef.Deutscher@grignon.inra.fr EP - 1031 TI - How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria. VL - 70 SP - 939 KW - background KW - carbohydrate KW - general KW - metabolism KW - phosphotransferase KW - phosphotransferase_system KW - pts KW - regulation AU - Deutscher, J AU - Francke, C AU - Postma, PW PY - 2006/12// UR - http://dx.doi.org/10.1128/MMBR.00024-06 ER -