Evidence against Stable Protein S-Nitrosylation as a Widespread Mechanism of Post-translational Regulation.

ABSTRACT: S-nitrosation, commonly referred to as S-nitrosylation, is widely regarded as a ubiquitous, stable post-translational modification that directly regulates many proteins. Such a widespread role would appear to be incompatible with the inherent lability of the S-nitroso bond, especially its propensity to rapidly react with thiols to generate disulfide bonds. As anticipated, we observed robust and widespread protein S-nitrosation after exposing cells to nitrosocysteine or lipopolysaccharide. Proteins detected using the ascorbate-dependent biotin switch method are typically interpreted to be directly regulated by S-nitrosation. However, these S-nitrosated proteins are shown to predominantly comprise transient intermediates leading to disulfide bond formation. These disulfides are likely to be

SUBMITTER: Wolhuter K 

PROVIDER: S-EPMC5807093 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature