Sumo modification system facilitates the exchange of histone variant h2a.Z-2 at dna damage sites

Atsuhiko Fukuto, Masae Ikura, Tsuyoshi Ikura, Jiying Sun, Yasunori Horikoshi, Hiroki Shima, Kazuhiko Igarashi, Masayuki Kusakabe, Masahiko Harata, Naoki Horikoshi, Hitoshi Kurumizaka, Yoshiaki Kiuchi, Satoshi Tashiro

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)87-94
Number of pages8
JournalNucleus
Volume9
Issue number1
DOIs
Publication statusPublished - 2018 Dec 12
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

Fingerprint Dive into the research topics of 'Sumo modification system facilitates the exchange of histone variant h2a.Z-2 at dna damage sites'. Together they form a unique fingerprint.

Cite this