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

Author:

Seth Divya1,Hausladen Alfred1,Wang Ya-Juan2,Stamler Jonathan S.1

Affiliation:

1. 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.

2. Center for Proteomics and Bioinformatics, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.

Abstract

Handling Nitrosative Stress S-nitrosylation of proteins is a principal mechanism of cellular signaling in eukaryotes but has not been reported in microbes. The transcription factor OxyR serves to protect bacterial cells from reactive oxygen species produced by cell metabolism in the presence of oxygen. Seth et al. (p. 470) found that when cells grew in the presence of nitrate, OxyR was modified by S-nitrosylation of the same cysteine residue that gets oxidized in cells grown aerobically. However, the nitrosylated OxyR activated a different set of genes—some of which appeared to protect the cell from excessive S-nitrosylation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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