Screening systems for the identification of S-nitrosylated proteins.

Takashi Uehara, Tadashi Nishiya

Journal: Nitric oxide : biology and chemistry 2011;25(2):108-11

PMID: 21111056

Full Text on Elsevier Science View on PubMed

Abstract

S-nitrosylation is a well-characterized reaction involving the covalent binding of nitric oxide (NO) to cysteine residues (Cys) in a protein. Similar to protein phosphorylation, S-nitrosylation is a post-translational modification involved in the regulation of a large number of intracellular functions and signaling events. Moreover, like phosphorylation, S-nitrosylation is precisely regulated in time and space. A procedure known as the biotin-switch method that specifically detects S-nitrosylated proteins (SNO-P) was recently developed by Snyder's group. They found that many proteins are substrates for NO, and several groups have attempted to identify other SNO-P by improving this method. In this review, we describe the SNO-P identified using modified versions of the biotin-switch method.

Address: Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japan. [email protected]

DOI: 10.1016/j.niox.2010.11.002

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MeSH Terms: Binding Sites, Biotin, Computational Biology, Cysteine, Disulfides, Mesylates, Nitric Oxide, Oxidation-Reduction, Protein Array Analysis, Protein Processing, Post-Translational, Proteins, Proteomics, S-Nitrosothiols, Substrate Specificity