Desensitization by covalent modification of the chemoreceptor of Escherichia coli.
Chemoreceptors in Escherichia coli were studied in situ in chemotactic mutants, deficient in the ability to modify the receptors, by using membrane vesicles prepared from the mutants. The affinity of the receptors for the ligands is related to the level of modification of the receptors. Unmodified serine receptor had a dissociation constant of 0.8 microM, while modified receptor had a dissociation constant that was at least 100-times higher. The results are discussed in relation to the two-state model of the chemoreceptor.
Yonekawa
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H
Hayashi
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H
D001224:Aspartic Acid / Q000378:metabolism; D001426:Bacterial Proteins; D002628:Chemoreceptor Cells / Q000187:drug effects / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D007700:Kinetics; D008745:Methylation; D009154:Mutation; D012694:Serine / Q000378:metabolism
D001426:Bacterial Proteins; D001224:Aspartic Acid; D012694:Serine