Kinetics of CheY phosphorylation by small molecule phosphodonors

Sandra S. Da Re, Dominique Deville-Bonne, Tatiana Tolstykh, Michel Véron, Jeffry B. Stock

Research output: Contribution to journalArticle

42 Scopus citations

Abstract

The chemotaxis response regulator CheY can acquire phosphoryl groups either from its associated autophosphorylating protein kinase, CheA, or from small phosphodonor molecules such as acetyl phosphate. We report a stopped-flow kinetic analysis of CheY phosphorylation by acetyl phosphate. The results show that CheY has a very low affinity for this phosphodonor (K(s)>>0.1 M), consistent with the conclusion that, whereas CheY provides catalytic functions for the phosphotransfer reaction, the CheA kinase may act simply to increase the effective phosphodonor concentration at the CheY active site. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)323-326
Number of pages4
JournalFEBS Letters
Volume457
Issue number3
DOIs
StatePublished - Sep 3 1999

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Keywords

  • Chemotaxis
  • Phosphotransfer
  • Two-component system

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