The ArcB sensor kinase of Escherichia coli autophosphorylates by an intramolecular reaction

J Bacteriol. 2010 Mar;192(6):1735-9. doi: 10.1128/JB.01401-09. Epub 2010 Jan 22.

Abstract

The Arc two-component system, comprising the ArcB sensor kinase and the ArcA response regulator, modulates the expression of numerous genes in response to the respiratory conditions of growth. ArcB is a tripartite histidine kinase whose activity is regulated by the oxidation of two cytosol-located redox-active cysteine residues that participate in intermolecular disulfide bond formation. Here we show that ArcB autophosphorylates through an intramolecular reaction which diverges from the usually envisaged intermolecular autophosphorylation of homodimeric histidine kinases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Binding Sites / physiology
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial / physiology*
  • Gene Expression Regulation, Enzymologic / physiology*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutation
  • Phosphorylation
  • Protein Kinases / genetics
  • Protein Kinases / metabolism*

Substances

  • Escherichia coli Proteins
  • Membrane Proteins
  • Adenosine Triphosphate
  • Protein Kinases
  • arcB protein, E coli