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Nucleus. 2018 Jan 1;9(1):87-94. doi: 10.1080/19491034.2017.1395543. Epub 2017 Dec 14.

SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites.

Author information

1
a Department of Cellular Biology , Research Institute for Radiation Biology and Medicine, Hiroshima University , Hiroshima , Japan.
2
b Department of Ophthalmology and Visual Science , Graduate School of Biomedical Sciences, Hiroshima University , Hiroshima , Japan.
3
c Laboratory of Chromatin Regulatory Network, Department of Mutagenesis , Radiation Biology Center, Kyoto University , Kyoto , Japan.
4
d Department of Biochemistry , Tohoku University Graduate School of Medicine , Sendai , Miyagi , Japan.
5
e Laboratory of Molecular Biology, Graduate School of Agricultural Science , Tohoku University , Sendai , Miyagi , Japan.
6
f Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering , Waseda University, Shinjukuku , Tokyo , Japan.
7
g Present address; Department of Structural Biology, School of Medicine , Stanford University , Stanford , CA , USA.

Abstract

Histone exchange and histone post-translational modifications play important roles in the regulation of DNA metabolism, by re-organizing the chromatin configuration. We previously demonstrated that the histone variant H2A.Z-2 is rapidly exchanged at damaged sites after DNA double strand break induction in human cells. In yeast, the small ubiquitin-like modifier (SUMO) modification of H2A.Z is involved in the DNA damage response. However, whether the SUMO modification regulates the exchange of human H2A.Z-2 at DNA damage sites remains unclear. Here, we show that H2A.Z-2 is SUMOylated in a damage-dependent manner, and the SUMOylation of H2A.Z-2 is suppressed by the depletion of the SUMO E3 ligase, PIAS4. Moreover, PIAS4 depletion represses the incorporation and eviction of H2A.Z-2 at damaged sites. These findings demonstrate that the PIAS4-mediated SUMOylation regulates the exchange of H2A.Z-2 at DNA damage sites.

KEYWORDS:

DNA damage; H2A.Z-2; PIAS4; SUMO; histone variant

PMID:
29095668
PMCID:
PMC5973225
DOI:
10.1080/19491034.2017.1395543
[Indexed for MEDLINE]
Free PMC Article

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