SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites. (1st January 2018)

• Record Type: Journal Article
• Authors: Fukuto, Atsuhiko; Ikura, Masae; Ikura, Tsuyoshi; Sun, Jiying; Horikoshi, Yasunori; Shima, Hiroki; Igarashi, Kazuhiko; Kusakabe, Masayuki; Harata, Masahiko; Horikoshi, Naoki; Kurumizaka, Hitoshi; Kiuchi, Yoshiaki; Tashiro, Satoshi
• Is Part Of: Nucleus. Volume 9:Number 1(2018)
• Page Start: 87
• Page End: 94
• Publication Date: 2018-01-01
• Subjects: H2A.Z-2 -- PIAS4 -- SUMO -- histone variant -- DNA damage; Cell nuclei -- Periodicals; Biology -- Periodicals; Biology; Cell nuclei; Periodicals; 571.6605
• DOI: 10.1080/19491034.2017.1395543
• Languages: English
• ISSNs: 1949-1034

Abstract

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.