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Article

Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis.

The Journal of biological chemistry - 5 May 1991

Lukat G S, Lee B H, Mottonen J M, Stock A M, Stock J B

Abstract excerpt

The chemotactic responses of bacteria such as Escherichia coli and Salmonella typhimurium are mediated by phosphorylation of the CheY protein. Phospho-CheY interacts with the flagellar motor switch to cause tumbly behavior. CheY belongs to a large family of phosphorylated response regulators that function in bacteria to control motility and regulate gene expression. Residues corresponding to Asp57, Asp13, and...

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Identifiers

PMID: 1902474

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis.PMID 1902474Read ↗

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

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

Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli.Semantic proximity Read ↗

Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY.Semantic proximity Read ↗

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

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

Synthesis and biochemical characterization of a phosphorylated analogue of the response regulator CheB.Semantic proximity Read ↗

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

Activation of CheY mutant D57N by phosphorylation at an alternative site, Ser-56.Semantic proximity Read ↗

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

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 ↗

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