Literature DB >> 22539721

Endogenous protein S-Nitrosylation in E. coli: regulation by OxyR.

Divya Seth1, Alfred Hausladen, Ya-Juan Wang, Jonathan S Stamler.   

Abstract

Endogenous S-nitrosylation of proteins, a principal mechanism of cellular signaling in eukaryotes, has not been observed in microbes. We report that protein S-nitrosylation is an obligate concomitant of anaerobic respiration on nitrate in Escherichia coli. Endogenous S-nitrosylation during anaerobic respiration is controlled by the transcription factor OxyR, previously thought to operate only under aerobic conditions. Deletion of OxyR resulted in large increases in protein S-nitrosylation, and S-nitrosylation of OxyR induced transcription from a regulon that is distinct from the regulon induced by OxyR oxidation. Furthermore, products unique to the anaerobic regulon protected against S-nitrosothiols, and anaerobic growth of E. coli lacking OxyR was impaired on nitrate. Thus, OxyR serves as a master regulator of S-nitrosylation, and alternative posttranslational modifications of OxyR control distinct transcriptional responses.

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Year:  2012        PMID: 22539721      PMCID: PMC3837355          DOI: 10.1126/science.1215643

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  26 in total

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Authors:  T W Overton; L Griffiths; M D Patel; J L Hobman; C W Penn; J A Cole; C Constantinidou
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3.  Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation.

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  66 in total

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