Redox-operated genetic switches: the SoxR and OxyR transcription factors

Trends Biotechnol. 2001 Mar;19(3):109-14. doi: 10.1016/s0167-7799(00)01542-0.

Abstract

Two redox-responsive transcription regulators have been well defined in Escherichia coli and serve as paradigms of redox-operated genetic switches. SoxR contains iron-sulfur centers that activate the protein when they are one-electron oxidized, or nitrosylated by nitric oxide. OxyR contains a pair of redox-active cysteine residues that activate the protein when they are oxidized to form a disulfide bond.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Biotechnology
  • DNA-Binding Proteins*
  • Disulfides / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins
  • Free Radicals / metabolism
  • Hydrogen Peroxide / metabolism
  • Nitric Oxide / metabolism
  • Oxidation-Reduction
  • Repressor Proteins / chemistry
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • Superoxides / metabolism
  • Transcription Factors / chemistry
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism*
  • Transcriptional Activation

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Disulfides
  • Escherichia coli Proteins
  • Free Radicals
  • Repressor Proteins
  • Transcription Factors
  • oxyR protein, E coli
  • Superoxides
  • SoxR protein, Bacteria
  • Nitric Oxide
  • Hydrogen Peroxide