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Direct Proteomic Mapping of Cysteine Persulfidation
Ling Fu1, Keke Liu1, Jingyang He1
1State Key Laboratory of Proteomics, Beijing Proteome Research Center, National Center for Protein Sciences • Beijing, Beijing Institute of Lifeomics, Beijing, China.
Antioxidants & Redox Signaling
|August 15, 2019
Summary
Cysteine persulfidation, a key redox mechanism, is now directly mapped using low-pH QTRP. This method identifies persulfidated sites in proteomes, revealing new insights into hydrogen sulfide signaling.
Area of Science:
- Biochemistry
- Proteomics
- Redox biology
Background:
- Cysteine persulfidation regulates protein function and biological processes via hydrogen sulfide (H2S) signaling.
- The instability of persulfidation poses challenges for its study and identification in complex proteomes.
- Existing methods require improvement for direct and unambiguous identification of persulfidated cysteine residues.
Purpose of the Study:
- To develop a quantitative chemoproteomic method for direct, site-specific mapping of persulfidated cysteine residues.
- To profile both persulfides and thiols simultaneously in complex biological samples.
- To establish a comprehensive inventory of persulfidation targets and analyze in vivo events.
Main Methods:
- Development of low-pH quantitative thiol reactivity profiling (QTRP).
- Application of QTRP to cell lysates treated with NaHS.
- Extension of QTRP to endogenous persulfides in cells, mouse tissues, and human serum.
Main Results:
- Identification of 1547 persulfidated sites on 994 proteins in NaHS-treated cell lysates.
- Discovery of unique consensus motifs associated with cysteine persulfidation.
- Profiling of endogenous persulfidation events, including detailed analysis of human serum albumin.
Conclusions:
- Low-pH QTRP is the first method for direct, unbiased proteomic mapping of cysteine persulfidation.
- The study provides the most comprehensive inventory of NaHS persulfidation targets to date.
- The method offers valuable insights into the biological functions of persulfidation through in vivo analysis.
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