The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining
Open accessAbstract
Given its significant role in the maintenance of genomic stability, histone methylation has been postulated to regulate DNA repair. Histone methylation mediates localization of 53BP1 to a DNA double-strand break (DSB) during homologous recombination repair, but a role in DSB repair by nonhomologous end-joining (NHEJ) has not been defined. By screening for histone methylation after DSB induction by ionizing radiation we found that generation of dimethyl histone H3 lysine 36 (H3K36me2) was the major event. Using a novel human cell system that rapidly generates a single defined DSB in the vast majority of cells, we found that the DNA repair protein Metnase (also SETMAR), which has a SET histone methylase domain, localized to an induced DSB and directly mediated the formation of H3K36me2 near the induced DSB. This dimethylation of H3K36 improved the association of early DNA repair components, including NBS1 and Ku70, with the induced DSB, and enhanced DSB repair. In addition, expression of JHDM1a (an H3K36me2 demethylase) or histone H3 in which K36 was mutated to A36 or R36 to prevent H3K36me2 formation decreased the association of early NHEJ repair components with an induced DSB and decreased DSB repair. Thus, these experiments define a histone methylation event that enhances DNA DSB repair by NHEJ.
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Cites
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884
Heterochromatic Genome Stability Requires Regulators of Histone H3 K9 Methylation
Peng, J. C., & Karpen, G. H. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000435 · Cited by 183
Cited by
Writing, erasing and reading histone lysine methylations
Hyun, K., Jeon, J., Park, K., & Kim, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.11 · Cited by 1,250
Booth, L. N., & Brunet, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.013 · Cited by 499
Mallette, F. A., Mattiroli, F., Cui, G., Young, L. C., Hendzel, M. J., Mer, G., Sixma, T. K., & Richard, S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.47 · Cited by 355
SET for life: biochemical activities and biological functions of SET domain-containing proteins
Herz, H.-M., Garruss, A., & Shilatifard, A. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.09.004 · Cited by 314
Marked for death: Targeting epigenetic changes in cancer
Pfister, S. X., & Ashworth, A. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.256 · Cited by 288
Metadata
- Authors
- Fnu, S., Williamson, E. A., De Haro, L. P., Brenneman, M., Wray, J., Shaheen, M., Radhakrishnan, K., Lee, S.-H., Nickoloff, J. A., & Hromas, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2010-12-27
- Volume
- 108
- Issue
- 2
- Pages
- 540-545
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2110002004
- Cited by
- 299
- References
- 2
- FWCI
- 6.26
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. https://app.cochat.ai/papers/10.1073/pnas.1013571108
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- Fnu, S., Williamson, E. A., De Haro, L. P., Brenneman, M., Wray, J., Shaheen, M., Radhakrishnan, K., Lee, S.-H., Nickoloff, J. A., & Hromas, R. (2011). Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1013571108
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