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. 1993 Apr;175(7):2097–2101. doi: 10.1128/jb.175.7.2097-2101.1993

The carboxy-terminal portion of the CheA kinase mediates regulation of autophosphorylation by transducer and CheW.

R B Bourret 1, J Davagnino 1, M I Simon 1
PMCID: PMC204313  PMID: 8384620

Abstract

The CheA kinase is a central protein in the signal transduction network that controls chemotaxis in Escherichia coli. CheA receives information from a transmembrane receptor (e.g., Tar) and CheW proteins and relays it to the CheB and CheY proteins. The biochemical activities of CheA proteins truncated at various distances from the carboxy terminus were examined. The carboxy-terminal portion of CheA regulates autophosphorylation in response to environmental signals transmitted through Tar and CheW. The central portion of CheA is required for autophosphorylation and is also presumably involved in dimer formation. The amino-terminal portion of CheA was previously shown to contain the site of autophosphorylation and to be able to transfer the phosphoryl group to CheB and CheY. These studies further delineate three functional domains of the CheA protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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