Response regulation in bacterial chemotaxis

Gudrun S. Lukat, Jeffry Benton Stock

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

The signal transduction system that mediates bacterial chemotaxis allows cells to moduate their swimming behavior in response to fluctuations in chemical stimuli. Receptors at the cell surface receive information from the surroundings. Signals are then passed from the receptors to cytoplasmic chemotaxis components: CheA, CheW, CheZ, CheR, and CheB. These proteins function to regulate the level of phosphorylation of a response regulator designated CheY that interacts with the flagellar motor switch complex to control swimming behavior. The structure of CheY has been determined. Magnesium ion is essential for activity. The active site contains highly conserved Asp residues that are required for divalent metal ion binding and CheY phosphorylation. Another residue‐at the active site, Lys109, is important in the phosphorylation‐induced conformational change that facilitates communication with the switch complex and another chemotaxis component, CheZ. CheZ facilitates the dephosphorylation of phospho‐CheY. Defects in CheY and CheZ can be suppressed by mutations in the flagellar switch complex. CheZ is thought to modulate the switch bias by varying the level of phospho‐CheY. © 1993 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)41-46
Number of pages6
JournalJournal of Cellular Biochemistry
Volume51
Issue number1
DOIs
StatePublished - Jan 1 1993

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Keywords

  • CheY
  • CheZ
  • histidine kinase
  • response regulators
  • switch complex

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