PMID:2677005
| Citation |
Lupas, A and Stock, J (1989) Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis. J. Biol. Chem. 264:17337-42 |
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| Abstract |
Two types of reversible protein modification reactions have been identified in bacterial chemotaxis, methylation of membrane receptor-transducer proteins at glutamate side chains and phosphorylation of cytoplasmic signal transduction proteins at histidine and aspartate side chains. CheB is a bifunctional enzyme that is involved in both these modification processes. Its C-terminal domain is a methylesterase that catalyzes the hydrolysis of gamma-carboxyl glutamyl methyl esters in the cytoplasmic domain of chemoreceptor proteins. Its N-terminal domain is a phosphatase that catalyzes the hydrolysis of phospho-CheA, the central response regulator of bacterial chemotaxis. Phospho-CheB, produced as an intermediate in the phosphatase reaction, has dramatically increased methylesterase activity. The interplay between the methylesterase and phosphatase activities of CheB may provide a crucial link between adaptation and excitation in stimulus-response coupling. |
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| Keywords |
Carboxylic Ester Hydrolases/metabolism; Chemotaxis/physiology; Cloning, Molecular; Enzyme Activation; Escherichia coli/enzymology; Kinetics; Methylation; Phosphorylation; Salmonella typhimurium/enzymology |
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