Polar location of the chemoreceptor complex in the Escherichia coli cell. Export

@article{1993Maddock, abstract = {The eukaryotic cell exhibits compartmentalization of functions to various membrane-bound organelles and to specific domains within each membrane. The spatial distribution of the membrane chemoreceptors and associated cytoplasmic chemotaxis proteins in Escherichia coli were examined as a prototypic functional aggregate in bacterial cells. Bacterial chemotaxis involves a phospho-relay system brought about by ligand association with a membrane receptor, culminating in a switch in the direction of flagellar rotation. The transduction of the chemotaxis signal is initiated by a chemoreceptor-CheW-CheA ternary complex at the inner membrane. These ternary complexes aggregate predominantly at the cell poles. Polar localization of the cytoplasmic CheA and CheW proteins is dependent on membrane-bound chemoreceptor. Chemoreceptors are not confined to the cell poles in strains lacking both CheA and CheW. The chemoreceptor-CheW binary complex is polarly localized in the absence of CheA, whereas the chemoreceptor-CheA binary complex is not confined to the cell poles in strains lacking CheW. The subcellular localization of the chemotaxis proteins may reflect a general mechanism by which the bacterial cell sequesters different regions of the cell for specialized functions.}, address = {Department of Developmental Biology, Beckman Center, Stanford University School of Medicine, CA 94305-5427.}, author = {Maddock, J. R. and Shapiro, L.}, citeulike-article-id = {1214653}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8456299}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8456299}, day = {19}, issn = {0036-8075}, journal = {Science}, keywords = {ch3, chemoreceptor, cluster, localisation, refs\_ox}, month = {March}, number = {5102}, pages = {1717--1723}, posted-at = {2007-04-07 10:25:24}, priority = {2}, title = {Polar location of the chemoreceptor complex in the Escherichia coli cell.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8456299}, volume = {259}, year = {1993} }

TY - JOUR ID - 1993Maddock L3 - citeulike-article-id:1214653 N2 - The eukaryotic cell exhibits compartmentalization of functions to various membrane-bound organelles and to specific domains within each membrane. The spatial distribution of the membrane chemoreceptors and associated cytoplasmic chemotaxis proteins in Escherichia coli were examined as a prototypic functional aggregate in bacterial cells. Bacterial chemotaxis involves a phospho-relay system brought about by ligand association with a membrane receptor, culminating in a switch in the direction of flagellar rotation. The transduction of the chemotaxis signal is initiated by a chemoreceptor-CheW-CheA ternary complex at the inner membrane. These ternary complexes aggregate predominantly at the cell poles. Polar localization of the cytoplasmic CheA and CheW proteins is dependent on membrane-bound chemoreceptor. Chemoreceptors are not confined to the cell poles in strains lacking both CheA and CheW. The chemoreceptor-CheW binary complex is polarly localized in the absence of CheA, whereas the chemoreceptor-CheA binary complex is not confined to the cell poles in strains lacking CheW. The subcellular localization of the chemotaxis proteins may reflect a general mechanism by which the bacterial cell sequesters different regions of the cell for specialized functions. IS - 5102 JF - Science SN - 0036-8075 AD - Department of Developmental Biology, Beckman Center, Stanford University School of Medicine, CA 94305-5427. EP - 1723 TI - Polar location of the chemoreceptor complex in the Escherichia coli cell. VL - 259 SP - 1717 KW - ch3 KW - chemoreceptor KW - cluster KW - localisation KW - refs_ox AU - Maddock, JR AU - Shapiro, L PY - 1993/03/19/ UR - http://view.ncbi.nlm.nih.gov/pubmed/8456299 ER -