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Phosphorylated HBO1 at UV irradiated sites is essential for nucleotide excision repair

Author

Listed:
  • Hiroyuki Niida

    (Hamamatsu University School of Medicine)

  • Ryoichi Matsunuma

    (Hamamatsu University School of Medicine
    Hamamatsu University School of Medicine)

  • Ryo Horiguchi

    (Advanced Research Facilities and Services, Preeminent Medical Photonics Education and Research Center, Hamamatsu University School of Medicine)

  • Chiharu Uchida

    (Advanced Research Facilities and Services, Preeminent Medical Photonics Education and Research Center, Hamamatsu University School of Medicine)

  • Yuka Nakazawa

    (Atomic Bomb Disease Institute, Nagasaki University)

  • Akira Motegi

    (Kyoto University Graduate School of Medicine)

  • Koji Nishimoto

    (Hamamatsu University School of Medicine)

  • Satoshi Sakai

    (Hamamatsu University School of Medicine)

  • Tatsuya Ohhata

    (Hamamatsu University School of Medicine)

  • Kyoko Kitagawa

    (Hamamatsu University School of Medicine)

  • Shinichi Moriwaki

    (Osaka Medical College)

  • Hideo Nishitani

    (Graduate School of Life Science, University of Hyogo)

  • Ayako Ui

    (St Marianna University, School of Medicine
    Institute of Medical Science, St Marianna University, School of Medicine
    School of Bioscience and Biotechnology, Tokyo University of Technology)

  • Tomoo Ogi

    (Research Institute of Environmental Medicine, Nagoya University, Furo-cho)

  • Masatoshi Kitagawa

    (Hamamatsu University School of Medicine
    Laboratory Animal Facilities and Services, Preeminent Medical Photonics Education and Research Center, Hamamatsu University School of Medicine)

Abstract

HBO1, a histone acetyl transferase, is a co-activator of DNA pre-replication complex formation. We recently reported that HBO1 is phosphorylated by ATM and/or ATR and binds to DDB2 after ultraviolet irradiation. Here, we show that phosphorylated HBO1 at cyclobutane pyrimidine dimer (CPD) sites mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites. Furthermore, HBO1 facilitates accumulation of SNF2H and ACF1, an ATP-dependent chromatin remodelling complex, to CPD sites. Depletion of HBO1 inhibited repair of CPDs and sensitized cells to ultraviolet irradiation. However, depletion of HBO1 in cells derived from xeroderma pigmentosum patient complementation groups, XPE, XPC and XPA, did not lead to additional sensitivity towards ultraviolet irradiation. Our findings suggest that HBO1 acts in concert with SNF2H–ACF1 to make the chromosome structure more accessible to canonical nucleotide excision repair factors.

Suggested Citation

  • Hiroyuki Niida & Ryoichi Matsunuma & Ryo Horiguchi & Chiharu Uchida & Yuka Nakazawa & Akira Motegi & Koji Nishimoto & Satoshi Sakai & Tatsuya Ohhata & Kyoko Kitagawa & Shinichi Moriwaki & Hideo Nishit, 2017. "Phosphorylated HBO1 at UV irradiated sites is essential for nucleotide excision repair," Nature Communications, Nature, vol. 8(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms16102
    DOI: 10.1038/ncomms16102
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