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Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.

08:00 EDT 12th October 2018 | BioPortfolio

Summary of "Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe."

Oxidation of a protein cysteinyl thiol (Cys-SH) to S-sulfenic acid (Cys-SOH) by a reactive oxygen species (e.g., hydrogen peroxide), which is termed protein S-sulfenylation, is a reversible post-translational modification that plays a crucial role in redox regulation of protein function in various biological processes. Due to its intrinsically labile nature, protein S-sulfenylation cannot be directly detected or analyzed. Chemoselective probing has been the method of choice for analyzing S-sulfenylated proteins either in vitro or in situ, as it allows stabilization and direct detection of this transient oxidative intermediate. However, it remains challenging to globally pinpoint the specific S-sulfenylated cysteine sites on complex proteomes and to quantify their dynamic changes upon oxidative stress. This unit describes how a benzothiazine-based chemoselective probe called BTD and mass spectrometry based chemoproteomics can be used to globally and site-specifically identify and quantify protein S-sulfenylation. © 2018 by John Wiley & Sons, Inc.

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This article was published in the following journal.

Name: Current protocols in protein science
ISSN: 1934-3663
Pages: e76

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