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Review
. 2018;17(21-22):2399-2410.
doi: 10.1080/15384101.2018.1542899. Epub 2018 Nov 14.

Histone modifications and the DNA double-strand break response

Hieu T Van  1 , Margarida A Santos  1
Affiliations
Review

Histone modifications and the DNA double-strand break response

Hieu T Van et al. Cell Cycle. 2018.

Abstract

The timely and precise repair of DNA damage, or more specifically DNA double-strand breaks (DSBs) - the most deleterious DNA lesions, is crucial for maintaining genome integrity and cellular homeostasis. An appropriate cellular response to DNA DSBs requires the integration of various factors, including the post-translational modifications (PTMs) of chromatin and chromatin-associated proteins. Notably, the PTMs of histones have been shown to play a fundamental role in initiating and regulating cellular responses to DNA DSBs. Here we review the role of the major histone PTMs, including phosphorylation, ubiquitination, methylation and acetylation, and their interactions during DNA DSB-induced responses.

Keywords: DNA damage; Histones; chromatin MODIFICATIONS.

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Figures

Figure 1.
Figure 1.
Histone modficiations and DNA double-strand break repair. (a) DNA double-strand breaks can be repaired by non-homologous end joining (NHEJ) or homologous recombination (HR). p53-binding protein 1 (53BP1) plays a crucial role in NHEJ, while breast cancer 1 (BRCA1) is important for HR. 53BP1 and BRCA1 mutually antagonize each other’s actions during the repair process.
Figure 2.
Figure 2.
The various functions of different post-translational modifications of histones in DNA damage responses. P: phosphorylation; deP: dephosphorylation; Ub: ubiquitination; Me: methylation; Ac: acetylation; deAc: deacetylation; H: histone; Lys: lysine; Ser: serine; Tyr: tyrosine.
Figure 3.
Figure 3.
The interplay of different histone modifications in generating and promoting the DNA damage response. Unbroken arrows illustrate the catalysis action of the proteins; broken arrows illustrate the recruitment of the proteins. P: phosphorylation; Ub: ubiquitination; Me: methylation; Ac: acetylation.
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