Interaction of Sirt3 with OGG1 contributes to repair of mitochondrial DNA and protects from apoptotic cell death under oxidative stress
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Sirtuin 3 (Sirt3), a major mitochondrial NAD(+)-dependent deacetylase, targets various mitochondrial proteins for lysine deacetylation and regulates important cellular functions such as energy metabolism, aging, and stress response. In this study, we identified the human 8-oxoguanine-DNA glycosylase 1 (OGG1), a DNA repair enzyme that excises 7,8-dihydro-8-oxoguanine (8-oxoG) from damaged genome, as a new target protein for Sirt3. We found that Sirt3 physically associated with OGG1 and deacetylated this DNA glycosylase and that deacetylation by Sirt3 prevented the degradation of the OGG1 protein and controlled its incision activity. We further showed that regulation of the acetylation and turnover of OGG1 by Sirt3 played a critical role in repairing mitochondrial DNA (mtDNA) damage, protecting mitochondrial integrity, and preventing apoptotic cell death under oxidative stress. We observed that following ionizing radiation, human tumor cells with silencing of Sirt3 expression exhibited deteriorated oxidative damage of mtDNA, as measured by the accumulation of 8-oxoG and 4977 common deletion, and showed more severe mitochondrial dysfunction and underwent greater apoptosis in comparison with the cells without silencing of Sirt3 expression. The results reported here not only reveal a new function and mechanism for Sirt3 in defending the mitochondrial genome against oxidative damage and protecting from the genotoxic stress-induced apoptotic cell death but also provide evidence supporting a new mtDNA repair pathway.
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Studies have indicated a role for SIRT3 in mediating tumor survival.
“On the other hand, studies have indicated a role in mediating tumor survival ((Alhazzazi et al. 2011);(Cheng et al. 2013)).”
From The Mitochondrial Acylome Emerges: Proteomics, Regulation by Sirtuins, and Metabolic and Disease Implications (2018) · cites this paper as Cheng et al. 2013
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Self-citation
- Authors
- Cheng, Y., Ren, X., Gowda, A. S., Shan, Y., Zhang, L., Yuan, Y.-S., Patel, R., Wu, H., Huber-Keener, K., Yang, J. W., Liu, D., Spratt, T. E., & Yang, J.-M.
- Affiliations
- Pennsylvania State University (US)
- Corresponding author
- Cheng, Y
- Yang, J W
- Yang, J-M
- Venue
- Cell Death & Disease
- Published
- 2013-07-18
- Volume
- 4
- Issue
- 7
- Pages
- e731-e731
- ISSN
- 2041-4889 (ISSN-L)
- PMC
- PMC3730425
- OpenAlex
- W1995450526
- Cited by
- 205
- References
- 48
- Citations by year
- 2026: 4 · 2025: 17 · 2024: 11 · 2023: 9 · 2022: 24 · 2021: 31 · 2020: 22 · 2019: 16 · 2018: 9 · 2017: 17 · 2016: 20 · 2015: 15 · 2014: 7 · 2013: 3
- FWCI
- 6.98
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- www.springer.com/tdm (unspecified)
- Locations
- Cell Death and Disease (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Defense
- Elsa U. Pardee Foundation (R01CA135038)
- National Cancer Institute (R01CA135038)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- SIRT3, OGG1, mitochondrial DNA repair, 8-oxoguanine, lysine deacetylation, protein stability, oxidative stress, apoptosis, ionizing radiation, mitochondrial dysfunction, genotoxic stress
- MeSH terms
- Acetylation, Calpain, DNA Damage, DNA Repair, DNA, Mitochondrial, Humans, Protein Binding, Protein Processing, Post-Translational, Apoptosis, Oxidative Stress, Protein Interaction Mapping, DNA Glycosylases, Cell Line, Tumor, Cell Proliferation, Membrane Potential, Mitochondrial, Gene Knockdown Techniques, Sirtuin 3, HEK293 Cells, Proteolysis
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