S-nitrosylation signaling in Escherichia coli

Sci Signal. 2012 Jun 12;5(228):pe26. doi: 10.1126/scisignal.2003181.


Most bacteria generate nitric oxide (NO) either aerobically by NO synthases or anaerobically from nitrite. Far from being a mere by-product of nitrate respiration, bacterial NO has diverse physiological roles. Many proteins undergo NO-mediated posttranslational modification (S-nitrosylation) in anaerobically grown Escherichia coli. The regulation of one such protein, OxyR, represents a redox signaling paradigm in which the same transcription factor controls different protective genes depending on its S-nitrosylation versus S-oxidation status. We discuss a structural model that may explain the remarkable stability and specificity of OxyR S-nitrosylation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / metabolism
  • Escherichia coli / physiology*
  • Escherichia coli Proteins / metabolism*
  • Models, Molecular*
  • Nitric Oxide / metabolism*
  • Protein Processing, Post-Translational / physiology*
  • Repressor Proteins / metabolism*
  • S-Nitrosothiols / metabolism*


  • Escherichia coli Proteins
  • Repressor Proteins
  • S-Nitrosothiols
  • oxyR protein, E coli
  • Nitric Oxide