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.
%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
}