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Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis

Nature volume 336, pages 139–143 (1988)Cite this article

Abstract

A cascade of protein phosphorylation, initiated by autophosphorylation of the CheA protein, may be important in the signal transduction pathway of bacterial chemotaxis. A proteolytic fragment of CheA cannot autophosphorylate, but can still transfer phosphate to proteins that generate excitation and adaptation signals. The site of CheA phosphorylation is His 48; mutants altered at this position are non-chemotactic. Similar mechanisms of transient protein phosphorylation and phosphoryl group transfer seem to be involved in processing sensory data and in activating specific gene expression.

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  1. Melvin I. Simon: To whom correspondence should be addressed.

Authors and Affiliations

  1. Division of Biology, California Institute of Technology, Pasadena, California, 91125, USA

    J. Fred Hess, Robert B. Bourret & Melvin I. Simon

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  1. J. Fred Hess
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  2. Robert B. Bourret
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  3. Melvin I. Simon
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Hess, J., Bourret, R. & Simon, M. Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis. Nature 336, 139–143 (1988). https://doi.org/10.1038/336139a0

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