Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration
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 structu...
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| Published in | Cell metabolism Vol. 30; no. 6; pp. 1152 - 1170.e13 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
03.12.2019
Elsevier |
| Subjects | |
| Online Access | Get full text |
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| Abstract | 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.
[Display omitted]
•Dimedone Switch method is a versatile, chemoselective persulfide labeling approach•Protein persulfidation is an evolutionarily conserved modification of cysteine thiols•Persulfidation waves rescue cysteines from overoxidation caused by ROS•Persulfidation decreases with aging, increases with caloric restriction, and extends lifespan
Zivanovic et al. develop a robust method for chemoselective persulfide labeling using dimedone-based probes to show that persulfidation is an evolutionarily conserved post-translational modification used by the cells to protect proteins from overoxidation caused by different stressors. Higher persulfidation levels, caused by pharmacological or dietary interventions, lead to better resistance to oxidative stress and longer life. |
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| AbstractList | Life on Earth emerged in a hydrogen sulfide (H
S)-rich environment eons ago and with it protein persulfidation mediated by H
S 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. 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.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. 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. [Display omitted] •Dimedone Switch method is a versatile, chemoselective persulfide labeling approach•Protein persulfidation is an evolutionarily conserved modification of cysteine thiols•Persulfidation waves rescue cysteines from overoxidation caused by ROS•Persulfidation decreases with aging, increases with caloric restriction, and extends lifespan Zivanovic et al. develop a robust method for chemoselective persulfide labeling using dimedone-based probes to show that persulfidation is an evolutionarily conserved post-translational modification used by the cells to protect proteins from overoxidation caused by different stressors. Higher persulfidation levels, caused by pharmacological or dietary interventions, lead to better resistance to oxidative stress and longer life. |
| Author | Kohl, Joshua B. Zivanovic, Jasmina Mitchell, James R. Adhikari, Bikash Benhar, Moran Carroll, Kate S. Petrovic, Dunja Filipovic, Milos R. Jung, Youngeun Schott-Roux, Sonia Gomes, Jose Eduardo Paul, Bindu D. Miler, Marko Miljkovic, Jan Lj Torregrossa, Roberta Snyder, Solomon H. Kouroussis, Emilia Whiteman, Matthew Milosevic, Verica Gonzalez-Zorn, Bruno Bursac, Biljana Thomas-Lopez, Daniel Schwarz, Guenter Mitchell, Sarah Ivanovic-Burmazovic, Ivana |
| Author_xml | – sequence: 1 givenname: Jasmina surname: Zivanovic fullname: Zivanovic, Jasmina organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 2 givenname: Emilia surname: Kouroussis fullname: Kouroussis, Emilia organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 3 givenname: Joshua B. surname: Kohl fullname: Kohl, Joshua B. organization: Department of Biochemistry, Center for Molecular Medicine, Institute of Biochemistry, University of Cologne, Cologne, Germany – sequence: 4 givenname: Bikash surname: Adhikari fullname: Adhikari, Bikash organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 5 givenname: Biljana surname: Bursac fullname: Bursac, Biljana organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 6 givenname: Sonia surname: Schott-Roux fullname: Schott-Roux, Sonia organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 7 givenname: Dunja surname: Petrovic fullname: Petrovic, Dunja organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 8 givenname: Jan Lj surname: Miljkovic fullname: Miljkovic, Jan Lj organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 9 givenname: Daniel surname: Thomas-Lopez fullname: Thomas-Lopez, Daniel organization: Departamento de Sanidad Animal, Facultad de Veterinaria and VISAVET, Universidad Complutense de Madrid, Madrid, Spain – sequence: 10 givenname: Youngeun surname: Jung fullname: Jung, Youngeun organization: Department of Chemistry, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA – sequence: 11 givenname: Marko surname: Miler fullname: Miler, Marko organization: Department of Cytology, Institute for Biological Research “Sinisa Stankovic”, National Institute of Republic of Serbia, University of Belgrade, Belgrade, Serbia – sequence: 12 givenname: Sarah surname: Mitchell fullname: Mitchell, Sarah organization: Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115, USA – sequence: 13 givenname: Verica surname: Milosevic fullname: Milosevic, Verica organization: Department of Cytology, Institute for Biological Research “Sinisa Stankovic”, National Institute of Republic of Serbia, University of Belgrade, Belgrade, Serbia – sequence: 14 givenname: Jose Eduardo surname: Gomes fullname: Gomes, Jose Eduardo organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France – sequence: 15 givenname: Moran surname: Benhar fullname: Benhar, Moran organization: Department of Biochemistry, Rappaport Institute for Research in the Medical Sciences, Faculty of Medicine, Technion – Israel Institute of Technology, Haifa 31096, Israel – sequence: 16 givenname: Bruno surname: Gonzalez-Zorn fullname: Gonzalez-Zorn, Bruno organization: Departamento de Sanidad Animal, Facultad de Veterinaria and VISAVET, Universidad Complutense de Madrid, Madrid, Spain – sequence: 17 givenname: Ivana surname: Ivanovic-Burmazovic fullname: Ivanovic-Burmazovic, Ivana organization: Department of Chemistry and Pharmacy, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany – sequence: 18 givenname: Roberta surname: Torregrossa fullname: Torregrossa, Roberta organization: University of Exeter Medical School, St. Luke's Campus, Exeter, UK – sequence: 19 givenname: James R. surname: Mitchell fullname: Mitchell, James R. organization: Department of Genetics and Complex Diseases, Harvard School of Public Health, Boston, MA 02115, USA – sequence: 20 givenname: Matthew surname: Whiteman fullname: Whiteman, Matthew organization: University of Exeter Medical School, St. Luke's Campus, Exeter, UK – sequence: 21 givenname: Guenter surname: Schwarz fullname: Schwarz, Guenter organization: Department of Biochemistry, Center for Molecular Medicine, Institute of Biochemistry, University of Cologne, Cologne, Germany – sequence: 22 givenname: Solomon H. surname: Snyder fullname: Snyder, Solomon H. organization: The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA – sequence: 23 givenname: Bindu D. surname: Paul fullname: Paul, Bindu D. organization: The Solomon H. Snyder Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA – sequence: 24 givenname: Kate S. surname: Carroll fullname: Carroll, Kate S. organization: Department of Chemistry, The Scripps Research Institute, 130 Scripps Way, Jupiter, FL 33458, USA – sequence: 25 givenname: Milos R. surname: Filipovic fullname: Filipovic, Milos R. email: milos.filipovic@ibgc.cnrs.fr organization: CNRS, Institut de Biochimie et Génétique Cellulaires UMR5095, Université de Bordeaux, Bordeaux, France |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/31735592$$D View this record in MEDLINE/PubMed https://hal.science/hal-03489073$$DView record in HAL |
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| Keywords | redox signaling protein persulfidation calorie restriction hydrogen sulfide sulfonylation hydrogen peroxide sulfinylation sulfenylation aging |
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| Snippet | 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... Life on Earth emerged in a hydrogen sulfide (H S)-rich environment eons ago and with it protein persulfidation mediated by H S evolved as a signaling... |
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| SubjectTerms | aging Aging - metabolism Animals Caenorhabditis elegans calorie restriction Cell Line Cyclohexanones - chemistry Cysteine - chemistry Cysteine - metabolism Drosophila melanogaster Escherichia coli Fibroblasts Humans hydrogen peroxide hydrogen sulfide Hydrogen Sulfide - metabolism Life Sciences Male Mice Mice, Inbred C57BL Oxidative Stress - physiology protein persulfidation Protein Processing, Post-Translational - physiology Rats Rats, Wistar redox signaling Saccharomyces cerevisiae Staining and Labeling sulfenylation Sulfides - metabolism sulfinylation sulfonylation |
| Title | Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration |
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