%0 Journal Article %1 Maddock1993 %A Maddock, %A Shapiro, L %D 1993 %J Science %K receptors ecoli chemotaxis %N 5102 %P 1717-1723 %R 10.1126/science.8456299 %T Polar location of the chemoreceptor complex in the Escherichia coli cell %U http://www.sciencemag.org/content/259/5102/1717.abstract %V 259 %X 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.

@article{Maddock1993, 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.}, added-at = {2013-05-31T15:02:33.000+0200}, author = {Maddock and Shapiro, L}, biburl = {https://www.bibsonomy.org/bibtex/29fd004c5c6384b8056efe942e046e61f/quantentunnel}, doi = {10.1126/science.8456299}, eprint = {http://www.sciencemag.org/content/259/5102/1717.full.pdf}, file = {Maddock1993.pdf:Artikel/Maddock1993.pdf:PDF}, groups = {public}, interhash = {138861255baae356d670ef51375aceef}, intrahash = {9fd004c5c6384b8056efe942e046e61f}, journal = {Science}, keywords = {receptors ecoli chemotaxis}, number = 5102, pages = {1717-1723}, timestamp = {2014-03-14T11:34:31.000+0100}, title = {Polar location of the chemoreceptor complex in the Escherichia coli cell}, url = {http://www.sciencemag.org/content/259/5102/1717.abstract}, username = {quantentunnel}, volume = 259, year = 1993 }