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 journalArticle

    5 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)1-8
    Number of pages8
    JournalNucleus
    DOIs
    Publication statusAccepted/In press - 2017 Dec 12

    Fingerprint

    Ubiquitin
    Histones
    Sumoylation
    DNA Damage
    Ubiquitin-Protein Ligases
    Double-Stranded DNA Breaks
    Post Translational Protein Processing
    Chromatin
    Yeasts
    DNA

    Keywords

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

    ASJC Scopus subject areas

    • Cell Biology

    Cite this

    Fukuto, A., Ikura, M., Ikura, T., Sun, J., Horikoshi, Y., Shima, H., ... Tashiro, S. (Accepted/In press). 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

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

    In: Nucleus, 12.12.2017, p. 1-8.

    Research output: Contribution to journalArticle

    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 2017, 'SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites', Nucleus, pp. 1-8. https://doi.org/10.1080/19491034.2017.1395543
    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. / SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites. In: Nucleus. 2017 ; pp. 1-8.
    @article{85eead017992444e8cc34b28a9a5a72b,
    title = "SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites",
    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, histone variant, PIAS4, SUMO",
    author = "Atsuhiko Fukuto and Masae Ikura and Tsuyoshi Ikura and Jiying Sun and Yasunori Horikoshi and Hiroki Shima and Kazuhiko Igarashi and Masayuki Kusakabe and Masahiko Harata and Naoki Horikoshi and Hitoshi Kurumizaka and Yoshiaki Kiuchi and Satoshi Tashiro",
    year = "2017",
    month = "12",
    day = "12",
    doi = "10.1080/19491034.2017.1395543",
    language = "English",
    pages = "1--8",
    journal = "Nucleus",
    issn = "0115-2300",
    publisher = "Landes Bioscience",

    }

    TY - JOUR

    T1 - SUMO modification system facilitates the exchange of histone variant H2A.Z-2 at DNA damage sites

    AU - Fukuto, Atsuhiko

    AU - Ikura, Masae

    AU - Ikura, Tsuyoshi

    AU - Sun, Jiying

    AU - Horikoshi, Yasunori

    AU - Shima, Hiroki

    AU - Igarashi, Kazuhiko

    AU - Kusakabe, Masayuki

    AU - Harata, Masahiko

    AU - Horikoshi, Naoki

    AU - Kurumizaka, Hitoshi

    AU - Kiuchi, Yoshiaki

    AU - Tashiro, Satoshi

    PY - 2017/12/12

    Y1 - 2017/12/12

    N2 - 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.

    AB - 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.

    KW - DNA damage

    KW - H2A.Z-2

    KW - histone variant

    KW - PIAS4

    KW - SUMO

    UR - http://www.scopus.com/inward/record.url?scp=85038104293&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=85038104293&partnerID=8YFLogxK

    U2 - 10.1080/19491034.2017.1395543

    DO - 10.1080/19491034.2017.1395543

    M3 - Article

    AN - SCOPUS:85038104293

    SP - 1

    EP - 8

    JO - Nucleus

    JF - Nucleus

    SN - 0115-2300

    ER -