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Abstract
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.
