S-nitrosylation signaling in Escherichia coli.
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.
Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA.
Ivan
I
Gusarov
Evgeny
E
Nudler
D004926:Escherichia coli / Q000378:metabolism / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008958:Models, Molecular; D009569:Nitric Oxide / Q000378:metabolism*; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D012097:Repressor Proteins / Q000378:metabolism*; D026403:S-Nitrosothiols / Q000378:metabolism*
D029968:Escherichia coli Proteins; D012097:Repressor Proteins; D026403:S-Nitrosothiols; C499299:oxyR protein, E coli; D009569:Nitric Oxide