Histidine phosphorylation and phosphoryl group transfer in bacterial chemotaxis

1 November 1988

journal article
research article
Published by Springer Nature in Nature

Vol. 336 (6195) , 139-143
https://doi.org/10.1038/336139a0

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.

Keywords

This publication has 49 references indexed in Scilit:

The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains
Science, 1988
Phosphorylation of three proteins in the signaling pathway of bacterial chemotaxis
Cell, 1988
Mutants defective in bacterial chemotaxis show modified protein phosphorylation
Cell, 1988
Sensory transduction in bacterial chemotaxis involves phosphotransfer between CHE proteins
Biochemical and Biophysical Research Communications, 1988
Phosphorus-31 nuclear magnetic resonance study of the active site phosphohistidine and regulatory phosphoserine residues of rat liver ATP-citrate lyase
Biochemistry, 1985
Reversibility of self-phosphorylation of a histidine residue of adrenocortical cyclic nucleotide-independent protein kinase, SPK 380
Biochemical and Biophysical Research Communications, 1983
Protein methylation in behavioural control mechanisms and in signal transduction
Nature, 1979
Change in direction of flagellar rotation is the basis of the chemotactic response in Escherichia coli
Nature, 1974
Flagellar rotation and the mechanism of bacterial motility
Nature, 1974
Phosphoramidic Acid and its Salts
Published by Wiley ,1972