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

Hiroyuki Niida (), Ryoichi Matsunuma, Ryo Horiguchi, Chiharu Uchida, Yuka Nakazawa, Akira Motegi, Koji Nishimoto, Satoshi Sakai, Tatsuya Ohhata, Kyoko Kitagawa, Shinichi Moriwaki, Hideo Nishitani, Ayako Ui, Tomoo Ogi and Masatoshi Kitagawa
Additional contact information
Hiroyuki Niida: Hamamatsu University School of Medicine
Ryoichi Matsunuma: 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
Tomoo Ogi: Research Institute of Environmental Medicine, Nagoya University, Furo-cho
Masatoshi Kitagawa: Hamamatsu University School of Medicine

Nature Communications, 2017, vol. 8, issue 1, 1-18

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms16102 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms16102

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms16102

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().