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

    研究成果: Article

    6 引用 (Scopus)

    抜粋

    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.

    元の言語English
    ページ(範囲)1-8
    ページ数8
    ジャーナルNucleus
    DOI
    出版物ステータスAccepted/In press - 2017 12 12

      フィンガープリント

    ASJC Scopus subject areas

    • Cell Biology

    これを引用

    Fukuto, A., Ikura, M., Ikura, T., Sun, J., Horikoshi, Y., Shima, H., Igarashi, K., Kusakabe, M., Harata, M., Horikoshi, N., Kurumizaka, H., Kiuchi, Y., & Tashiro, S. (受理済み/印刷中). SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites. Nucleus, 1-8. https://doi.org/10.1080/19491034.2017.1395543