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