期刊
CHEMBIOCHEM
卷 18, 期 20, 页码 2028-2032出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201700137
关键词
cysteine; Michael addition; protein modifications; redox chemistry; sulfur
资金
- National Institutes of Health [DP2 GM114848, T32 CA140044, T32 GM008597, S10 OD021619]
- National Science Foundation Graduate Research Fellowship
- American Heart Association [14POST20420040]
- University of Michigan
Cysteine residues are susceptible to oxidation to form S-sulfinyl (R-SO2H) and S-sulfonyl (R-SO3H) post-translational modifications. Here we present a simple bioconjugation strategy to label S-sulfinated proteins by using reporter-linked maleimides. After alkylation of free thiols with iodoacetamide, S-sulfinated cysteines react with maleimide to form a sulfone Michael adduct that remains stable under acidic conditions. Using this sequential alkylation strategy, we demonstrate differential S-sulfination across mouse tissue homogenates, as well as enhanced S-sulfination following pharmacological induction of endoplasmic reticulum stress, lipopolysaccharide stimulation, and inhibitors of the electron transport chain. Overall, this study reveals a broadened profile of maleimide reactivity across cysteine modifications, and outlines a simple method for profiling the physiological role of cysteine S-sulfination in disease.
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