Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration
Autor: | Jasmina Zivanovic, Sonia Schott-Roux, James R. Mitchell, Bikash Adhikari, Biljana Bursac, Guenter Schwarz, Jan Lj. Miljkovic, Sarah J. Mitchell, Bindu D. Paul, Daniel Thomas-Lopez, Milos R. Filipovic, Ivana Ivanović-Burmazović, Moran Benhar, Joshua B. Kohl, Roberta Torregrossa, José-Eduardo Gomes, Solomon H. Snyder, Bruno Gonzalez-Zorn, Kate S. Carroll, Matthew Whiteman, Verica Milošević, Youngeun Jung, Marko Miler, Emilia Kouroussis, Dunja Petrovic |
---|---|
Přispěvatelé: | Institut de biochimie et génétique cellulaires (IBGC), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS) |
Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
Sulfenylation
0301 basic medicine Male Aging Redox signaling Physiology [SDV]Life Sciences [q-bio] Protein persulfidation Mice Protein structure 0302 clinical medicine Hydrogen Sulfide 2. Zero hunger Protein function 0303 health sciences Hydrogen sulfide Gasotransmitters Chemistry Highly selective Cell biology Pharmacological interventions Cell metabolism Drosophila melanogaster Signal Transduction Saccharomyces cerevisiae Sulfides Article Cell Line 03 medical and health sciences Escherichia coli Animals Humans Cysteine Rats Wistar Caenorhabditis elegans Molecular Biology Sulfonylation Calorie restriction 030304 developmental biology Bioconjugation Staining and Labeling Cyclohexanones Cell Biology Fibroblasts Hydrogen peroxide Rats Mice Inbred C57BL Oxidative Stress 030104 developmental biology Protein Processing Post-Translational Sulfinylation Function (biology) 030217 neurology & neurosurgery |
Zdroj: | Cell Metab Cell Metabolism Cell Metabolism, Elsevier, 2019, 30, pp.1152-1170.e13. ⟨10.1016/j.cmet.2019.10.007⟩ |
ISSN: | 1550-4131 |
DOI: | 10.1016/j.cmet.2019.10.007⟩ |
Popis: | Summary Life on Earth emerged in a hydrogen sulfide (H2S)-rich environment eons ago and with it protein persulfidation mediated by H2S evolved as a signaling mechanism. Protein persulfidation (S-sulfhydration) is a post-translational modification of reactive cysteine residues, which modulate protein structure and/or function. Persulfides are difficult to label and study due to their reactivity and similarity with cysteine. Here, we report a facile strategy for chemoselective persulfide bioconjugation using dimedone-based probes, to achieve highly selective, rapid, and robust persulfide labeling in biological samples with broad utility. Using this method, we show persulfidation is an evolutionarily conserved modification and waves of persulfidation are employed by cells to resolve sulfenylation and prevent irreversible cysteine overoxidation preserving protein function. We report an age-associated decline in persulfidation that is conserved across evolutionary boundaries. Accordingly, dietary or pharmacological interventions to increase persulfidation associate with increased longevity and improved capacity to cope with stress stimuli. |
Databáze: | OpenAIRE |
Externí odkaz: |