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Chemical proteomics reveals new targets of cysteine sulfinic acid reductase
- Source :
- Nature Chemical Biology. 14:995-1004
- Publication Year :
- 2018
- Publisher :
- Springer Science and Business Media LLC, 2018.
-
Abstract
- Cysteine sulfinic acid or S-sulfinylation is an oxidative post-translational modification (OxiPTM) that is known to be involved in redox-dependent regulation of protein function but has been historically difficult to analyze biochemically. To facilitate the detection of S-sulfinylated proteins, we demonstrate that a clickable, electrophilic diazene probe (DiaAlk) enables capture and site-centric proteomic analysis of this OxiPTM. Using this workflow, we revealed a striking difference between sulfenic acid modification (S-sulfenylation) and the S-sulfinylation dynamic response to oxidative stress, which is indicative of different roles for these OxiPTMs in redox regulation. We also identified >55 heretofore-unknown protein substrates of the cysteine sulfinic acid reductase sulfiredoxin, extending its function well beyond those of 2-cysteine peroxiredoxins (2-Cys PRDX1-4) and offering new insights into the role of this unique oxidoreductase as a central mediator of reactive oxygen species-associated diseases, particularly cancer. DiaAlk therefore provides a novel tool to profile S-sulfinylated proteins and study their regulatory mechanisms in cells.
- Subjects :
- Proteomics
0301 basic medicine
Nitrogen
Oxidative phosphorylation
Reductase
medicine.disease_cause
Sulfenic Acids
Epitopes
03 medical and health sciences
chemistry.chemical_compound
Oxidoreductase
medicine
Humans
Oxidoreductases Acting on Sulfur Group Donors
Cysteine
Molecular Biology
chemistry.chemical_classification
030102 biochemistry & molecular biology
Chemistry
Peroxiredoxins
Cell Biology
Recombinant Proteins
3. Good health
Oxidative Stress
Sulfiredoxin
HEK293 Cells
030104 developmental biology
Biochemistry
A549 Cells
Cysteine sulfinic acid
Sulfenic acid
Peptides
Reactive Oxygen Species
Oxidation-Reduction
Protein Processing, Post-Translational
Oxidative stress
HeLa Cells
Subjects
Details
- ISSN :
- 15524469 and 15524450
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Nature Chemical Biology
- Accession number :
- edsair.doi.dedup.....f0a5fed65216888faf95e9ce82ac58b0