Open AccessProteome‐Wide Analysis of Cysteine S‐Sulfenylation Using a Benzothiazine‐Based Probe
Author(s) -
Fu Ling,
Liu Keke,
Ferreira Renan B.,
Carroll Kate S.,
Yang Jing
Publication year - 2019
Publication title -
current protocols in protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.409
H-Index - 32
eISSN - 1934-3663
pISSN - 1934-3655
DOI - 10.1002/cpps.76
Subject(s) - sulfenic acid , chemistry , cysteine , proteome , benzothiazine , hydrogen peroxide , proteomics , biochemistry , oxidative phosphorylation , thiol , reactive oxygen species , combinatorial chemistry , oxidative stress , biophysics , enzyme , organic chemistry , biology , gene
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.