Two-component signal transduction

Ann Stock, V. L. Robinson, P. N. Goudreau

Research output: Contribution to journalReview article

2123 Scopus citations

Abstract

Most prokaryotic signal-transduction systems and a few eukaryotic pathways use phosphotransfer schemes involving two conserved components, a histidine protein kinase and a response regulator protein. The histidine protein kinase, which is regulated by environmental stimuli, autophosphorylates at a histidine residue, creating a high-energy phosphoryl group that is subsequently transferred to an aspartate residue in the response regulator protein. Phosphorylation induces a conformational change in the regulatory domain that results in activation of an associated domain that effects the response. The basic scheme is highly adaptable, and numerous variations have provided optimization within specific signaling systems. The domains of two-component proteins are modular and can be integrated into proteins and pathways in a variety of ways, but the core structures and activities are maintained. Thus detailed analyses of a relatively small number of representative proteins provide a foundation for understanding this large family of signaling proteins.

Original languageEnglish (US)
Pages (from-to)183-215
Number of pages33
JournalAnnual review of biochemistry
Volume69
DOIs
StatePublished - Nov 2 2000

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All Science Journal Classification (ASJC) codes

  • Biochemistry

Keywords

  • Gene expression
  • Histidine protein kinase
  • Phosphorylation
  • Protein conformational change
  • Response regulator

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