Detection of Protein S-Sulfhydration by a Tag-Switch Technique
Autor: | Dehui Zhang, Jia Pan, Chung-Min Park, Milos R. Filipovic, Nelmi O. Devarie-Baez, Ming Xian, Igor Macinkovic, Kate S. Carroll |
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Rok vydání: | 2013 |
Předmět: |
Biotin
Oxidative phosphorylation Sulfides Article Catalysis Protein S Adduct Jurkat Cells chemistry.chemical_compound Thioether Human Umbilical Vein Endothelial Cells Humans Cysteine Hydrogen Sulfide Sulfhydryl Compounds Glutathione Peroxidase biology Serum Albumin Bovine General Chemistry equipment and supplies Microscopy Fluorescence Biochemistry chemistry Posttranslational modification biology.protein Sulfenic acid Signal transduction Protein Processing Post-Translational |
Zdroj: | Angewandte Chemie International Edition. 53:575-581 |
ISSN: | 1433-7851 |
DOI: | 10.1002/anie.201305876 |
Popis: | Protein S-sulfhydration (forming -S-SH adducts from cysteine residues) is a newly defined oxidative posttranslational modification and plays an important role in H2 S-mediated signaling pathways. In this study we report the first selective, "tag-switch" method which can directly label protein S-sulfhydrated residues by forming stable thioether conjugates. Furthermore we demonstrate that H2 S alone cannot lead to S-sulfhydration and that the two possible physiological mechanisms include reaction with protein sulfenic acids (P-SOH) or the involvement of metal centers which would facilitate the oxidation of H2 S to HS(.) . |
Databáze: | OpenAIRE |
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