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Nature. 1988 Nov 10;336(6195):139-43.

Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis.

Author information

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

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.

PMID:
3185734
DOI:
10.1038/336139a0
[Indexed for MEDLINE]

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