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Article

Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ.

Biochemistry - 1 Feb 1994

Blat Y, Eisenbach M

Abstract excerpt

Bacterial chemotaxis is accomplished by regulating the direction of flagellar rotation. The primary target of the control appears to be CheY, a diffusible clockwise-signal molecule which interacts with the switch at the base of the flagellar motor and causes clockwise rotation. The regulatory mechanism appears to be phosphorylation/dephosphorylation of CheY. Here we demonstrate that CheZ, which accelerates the...

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Identifiers

PMID: 8305438
DOI: 10.1021/bi00170a008

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Phosphorylation-dependent binding of the chemotaxis signal molecule CheY to its phosphatase, CheZ.PMID 8305438Read ↗

Interaction of CheY with the C-terminal peptide of CheZ.Semantic proximity Read ↗

Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Semantic proximity Read ↗

Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ.Semantic proximity Read ↗

Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.Semantic proximity Read ↗

CheX in the three-phosphatase system of bacterial chemotaxis.Semantic proximity Read ↗

Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY.Semantic proximity Read ↗

Structure and function of an unusual family of protein phosphatases: the bacterial chemotaxis proteins CheC and CheX.Semantic proximity Read ↗

Role of Position K+4 in the Phosphorylation and Dephosphorylation Reaction Kinetics of the CheY Response Regulator.Semantic proximity Read ↗

Bacillus subtilis CheC and FliY are members of a novel class of CheY-P-hydrolyzing proteins in the chemotactic signal transduction cascade.Semantic proximity Read ↗

In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants.Semantic proximity Read ↗

Correlated switch binding and signaling in bacterial chemotaxis.Semantic proximity Read ↗

Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis.Semantic proximity Read ↗

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