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A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
Abstract
DNA breaks are extremely harmful lesions that need to be repaired efficiently throughout the genome. However, the packaging of DNA into nucleosomes is a significant barrier to DNA repair, and the mechanisms of repair in the context of chromatin are poorly understood. Here we show that lysine 56 (K56) acetylation is an abundant modification of newly synthesized histone H3 molecules that are incorporated into chromosomes during S phase. Defects in the acetylation of K56 in histone H3 result in sensitivity to genotoxic agents that cause DNA strand breaks during replication. In the absence of DNA damage, the acetylation of histone H3 K56 largely disappears in G2. In contrast, cells with DNA breaks maintain high levels of acetylation, and the persistence of the modification is dependent on DNA damage checkpoint proteins. We suggest that the acetylation of histone H3 K56 creates a favourable chromatin environment for DNA repair and that a key component of the DNA damage response is to preserve this acetylation.
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“The in vitro acetylation of lysine residues seems to be highly specific, in that only those lysine residues that are normally acetylated in vivo can also be acetylated in vitro following incubation with an acetyl-CoA:lysine acetyltransferase (Masumoto scientific report et al, 2005;Yuan et al, 2005;Costantini et al, 2007).”
From PCSK9 is required for the disposal of non-acetylated intermediates of the nascent membrane protein BACE1 (2008) · cites this paper as Masumoto et al, 2005
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Cited by
Sorted by citations
Histone core modifications regulating nucleosome structure and dynamics
Tessarz, P., & Kouzarides, T. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3890 · Cited by 1,018
Collins, S. R., Miller, K. M., Maas, N. L., Roguev, A., Fillingham, J., Chu, C. S., Schuldiner, M., Gebbia, M., Recht, J., Shales, M., et al. (2007) · Nature · doi:10.1038/nature05649 · Cited by 869
Cai, L., Sutter, B. M., Li, B., & Tu, B. P. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.004 · Cited by 701
Aguilera, A., & García-Muse, T. (2013) · Annual Review of Genetics · doi:10.1146/annurev-genet-111212-133232 · Cited by 476
Acetylation of Histone H3 Lysine 56 Regulates Replication-Coupled Nucleosome Assembly
Li, Q., Zhou, H., Wurtele, H., Davies, B., Horazdovsky, B., Verreault, A., & Zhang, Z. (2008) · Cell · doi:10.1016/j.cell.2008.06.018 · Cited by 447
Self-citation
Metadata
- Authors
- Masumoto, H., Hawke, D., Kobayashi, R., & Verreault, A.
- Venue
- Nature
- Published
- 2005-07
- Volume
- 436
- Issue
- 7048
- Pages
- 294-298
- ISSN
- 0028-0836
- 1476-4687
- Cited by
- 544
- References
- 1
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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