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Phosphorylation of an N-terminal Regulatory Domain Activates the CheB Methylesterase in Bacterial Chemotaxis

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Lupas, A, Stock, J·1989·Journal of Biological Chemistry

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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Metadata

Authors
Lupas, A., & Stock, J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1989-10
Volume
264
Issue
29
Pages
17337-17342
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1556270322
Cited by
194
References
0
FWCI
5.03
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Phosphorylation of an N-terminal Regulatory Domain Activates the CheB Methylesterase in Bacterial Chemotaxis. https://app.cochat.ai/papers/10.1016/s0021-9258(18)71497-x
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Lupas, A., & Stock, J. (1989). Phosphorylation of an N-terminal Regulatory Domain Activates the CheB Methylesterase in Bacterial Chemotaxis. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)71497-x

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