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Profiling Protein S-Sulfination with Maleimide-Linked Probes
Yu-Hsuan Kuo1, Aaron M Konopko1, Nicholas B Borotto1
1Program in Chemical Biology, Department of Chemistry, University of Michigan, Ann Arbor, MI, 48109, USA.
Chembiochem : a European Journal of Chemical Biology
|August 16, 2017
Summary
Researchers developed a bioconjugation method to detect S-sulfinated proteins, revealing diverse cysteine modifications and their roles in disease. This technique aids in understanding protein oxidation and its physiological implications.
Area of Science:
- Biochemistry
- Proteomics
- Chemical Biology
Background:
- Cysteine residues undergo oxidation to form S-sulfinyl and S-sulfonyl post-translational modifications.
- Understanding these modifications is crucial for deciphering cellular signaling and disease pathogenesis.
Purpose of the Study:
- To develop a straightforward bioconjugation strategy for labeling and profiling S-sulfinated proteins.
- To investigate the physiological relevance of cysteine S-sulfination in various biological contexts.
Main Methods:
- Sequential alkylation of free thiols with iodoacetamide.
- Subsequent reaction of S-sulfinated cysteines with reporter-linked maleimides to form stable sulfone adducts.
- Analysis of differential S-sulfination patterns in mouse tissue homogenates.
Main Results:
- Demonstrated successful labeling of S-sulfinated proteins using maleimide chemistry.
- Observed differential S-sulfination patterns across mouse tissues.
- Showed enhanced S-sulfination under conditions of endoplasmic reticulum stress, lipopolysaccharide stimulation, and electron transport chain inhibition.
Conclusions:
- Established a versatile bioconjugation method applicable to various cysteine modifications, broadening maleimide reactivity.
- Provided a simple approach for profiling cysteine S-sulfination, facilitating the study of its physiological roles in disease.
