The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability
Open accessAbstract
Although SIRT7 is a member of sirtuin family proteins that are described as NAD+-dependent class III histone deacetylases, the intrinsic enzymatic activity of this sirtuin protein remains to be investigated and the cellular function of SIRT7 remains to be explored. Here we report that SIRT7 is an NAD+-dependent histone desuccinylase. We show that SIRT7 is recruited to DNA double-strand breaks (DSBs) in a PARP1-dependent manner and catalyses desuccinylation of H3K122 therein, thereby promoting chromatin condensation and DSB repair. We demonstrate that depletion of SIRT7 impairs chromatin compaction during DNA-damage response and sensitizes cells to genotoxic stresses. Our study indicates SIRT7 is a histone desuccinylase, providing a molecular basis for the understanding of epigenetic regulation by this sirtuin protein. Our experiments reveal that SIRT7-catalysed H3K122 desuccinylation is critically implemented in DNA-damage response and cell survival, providing a mechanistic insight into the cellular function of SIRT7.
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Cites
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
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The language of covalent histone modifications
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Genome-scale CRISPR-Cas9 knockout screening in human cells
Shalem, O., Sanjana, N. E., Hartenian, E., Shi, X., Scott, D. A., Mikkelsen, T. S., Heckl, D., Ebert, B. L., Root, D. E., Doench, J. G., et al. (2014) · Science · doi:10.1126/science.1247005 · Cited by 5,234
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Self-citationThe Sir2 Family of Protein Deacetylases
Blander, G., & Guarente, L. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073651 · Cited by 1,495
Solvent Mediated Interactions in the Structure of the Nucleosome Core Particle at 1.9Å Resolution
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Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase
Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429
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β-Hydroxybutyrate: A Signaling Metabolite
Newman, J. C., & Verdin, E. (2017) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071816-064916 · Cited by 872
“Lysine succinylation is another histone posttranslational modification (147) and is regulated by the sirtuin SIRT7 in the context of the DNA damage response (73).”
Metabolic reprogramming and epigenetic modifications on the path to cancer
Sun, L., Zhang, H., & Gao, P. (2022) · Protein & Cell · doi:10.1007/s13238-021-00846-7 · Cited by 770
Self-citationZhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
Compartmentalised acyl-CoA metabolism and roles in chromatin regulation
Trefely, S., Lovell, C. D., Snyder, N. W., & Wellen, K. E. (2020) · Molecular Metabolism · doi:10.1016/j.molmet.2020.01.005 · Cited by 272
Metabolic adaptation in hypoxia and cancer
Paredes, F., Williams, H. C., & San Martin, A. (2021) · Cancer Letters · doi:10.1016/j.canlet.2020.12.020 · Cited by 259
Metadata
- Authors
- Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., He, L., Li, W., Yi, X., Sun, L., Liang, J., Cheng, Z., Shi, L., Shang, Y., & Yu, W.
- Venue
- Nature Communications
- Published
- 2016-07-20
- Volume
- 7
- Issue
- 1
- Pages
- 12235-12235
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2485886299
- Cited by
- 391
- References
- 70
- FWCI
- 15.80
- Type
- journal article
- Language
- en
- Open access
- gold
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- Li, L., Shi, L., Yang, S., Yan, R., Zhang, D., Yang, J., He, L., Li, W., Yi, X., Sun, L., Liang, J., Cheng, Z., Shi, L., Shang, Y., & Yu, W. (2016). SIRT7 is a histone desuccinylase that functionally links to chromatin compaction and genome stability. Nature Communications. https://doi.org/10.1038/ncomms12235
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