The Saccharomyces cerevisiae Proteome of Oxidized Protein Thiols
Open accessAbstract
Protein thiol oxidation subserves important biological functions and constitutes a sequel of reactive oxygen species toxicity. We developed two distinct thiol-labeling approaches to identify oxidized cytoplasmic protein thiols in Saccharomyces cerevisiae. Inone approach, we used N-(6-(biotinamido)hexyl)-3'-(2'-pyridyldithio)-propionamide to purify oxidized protein thiols, and in the other, we used N-[(14)C]ethylmaleimide to quantify this oxidation. Both approaches showed a large number of the same proteins with oxidized thiols ( approximately 200), 64 of which were identified by mass spectrometry. We show that, irrespective of its mechanism, protein thiol oxidation is dependent upon molecular O(2). We also show that H(2)O(2) does not cause de novo protein thiol oxidation, but rather increases the oxidation state of a select group of proteins. Furthermore, our study reveals contrasted differences in the oxidized proteome of cells upon inactivation of the thioredoxin or GSH pathway suggestive of very distinct thiol redox control functions, assigning an exclusive role for thioredoxin in H(2)O(2) metabolism and the presumed thiol redox buffer function for GSH. Taken together, these results suggest the high selectivity of cytoplasmic protein thiol oxidation.
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In yeast, anaerobic growth substantially decreased detection of proteins with sulfenic acid or disulfide bonds.
“studies in yeast, for example, found that anaerobic growth substantially decreased detection of proteins with sulfenic acid or disulfide bonds (234).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [234]
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- Authors
- Le Moan, N., Clement, G., Le Maout, S., Tacnet, F., & Toledano, M. B.
- Affiliations
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-04
- Volume
- 281
- Issue
- 15
- Pages
- 10420-10430
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2161861367
- Cited by
- 170
- References
- 54
- Citations by year
- 2025: 7 · 2024: 7 · 2022: 4 · 2021: 5 · 2020: 6 · 2019: 7 · 2018: 2 · 2017: 8 · 2016: 7 · 2015: 7 · 2014: 12 · 2013: 7 · 2012: 8
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Association pour la Recherche sur le Cancer
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- protein thiol oxidation, cytosolic proteins, Saccharomyces cerevisiae, thiol labeling, N-ethylmaleimide, reactive oxygen species, hydrogen peroxide, oxygen dependence, thioredoxin, glutathione, thiol redox regulation
- MeSH terms
- Biotin, Carbohydrates, Cytoplasm, Disulfides, Dithiothreitol, Glutathione, Hydrogen Peroxide, Hydrogen-Ion Concentration, Models, Chemical, Oxidation-Reduction, Oxygen, Plasmids, Saccharomyces cerevisiae, Mass Spectrometry, Sulfhydryl Compounds, Thioredoxins, Blotting, Western, Electrophoresis, Gel, Two-Dimensional, Reactive Oxygen Species, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Glutathione Disulfide, Saccharomyces cerevisiae Proteins, Proteomics
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