Endogenous protein S-Nitrosylation in E. coli: regulation by OxyR.
Summary of "Endogenous protein S-Nitrosylation in E. coli: regulation by OxyR."
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.
Institute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University School of Medicine and University Hospitals Case Medical Center, Cleveland, OH 44106, USA.
This article was published in the following journal.
Name: Science (New York, N.Y.)
- PubMed Source: http://www.ncbi.nlm.nih.gov/pubmed/22539721
- DOI: http://dx.doi.org/10.1126/science.1215643
Medical and Biotech [MESH] Definitions
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Enterohemorrhagic Escherichia Coli
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Adenomatous Polyposis Coli Protein
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