Work

Endogenous Protein S-Nitrosylation in E. coli : Regulation by OxyR

Year: 2012

Type: article

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.

Source: Science

DOI: 10.1126/science.1215643

Authors: Divya Seth, Alfred Hausladen, Ya-Juan Wang, Jonathan S. Stamler

Institutions: University Hospitals Cleveland Medical Center, Case Western Reserve University

Language: English

Topic: Redox biology and oxidative stress

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Heart, Lung, and Blood Institute

Awards: Restoration and Function of S-nitrosothiol in Stored Blood, Redox Signalling by Nitric Oxide in Skeletal Muscle, Regulation of Cardiac Adrenergic Function by S-nitrosylation