Cited by 44DNA Repair MechanismsGenomics and Chromatin DynamicsChromatin Remodeling and Cancer

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

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Niida, Hiroyuki, Matsunuma, Ryoichi, Horiguchi, Ryo, Uchida, Chiharu, Nakazawa, Yuka, Motegi, Akira, Nishimoto, Koji, Sakai, Satoshi +7 more·2017·Nature Communications

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.

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  1. Kraemer K. H.. Genetic heterogeneity in xeroderma pigmentosum: complementation groups and their relationship to DNA repair rates. Proc. Natl Acad. Sci. USA 72, 59– 63 (1975). 164028 PMC432240

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Authors
Niida, H., Matsunuma, R., Horiguchi, R., Uchida, C., Nakazawa, Y., Motegi, A., Nishimoto, K., Sakai, S., Ohhata, T., Kitagawa, K., Moriwaki, S., Nishitani, H., Ui, A., Ogi, T., & Kitagawa, M.
Affiliations
  • Hamamatsu University (JP)
  • Nagasaki University (JP)
  • Kyoto University (JP)
  • University of Hyogo (JP)
  • Tokyo University of Technology (JP)
  • Research Institute of Environmental Medicine, Nagoya University (JP)
Corresponding author
Niida, Hiroyuki
Venue
Nature Communications
Published
2017-07-18
Volume
8
Issue
1
Pages
16102-16102
ISSN
2041-1723 (ISSN-L)
OpenAlex
W2736444859
Cited by
44
References
52
Citations by year
2026: 3 · 2025: 6 · 2024: 7 · 2023: 4 · 2022: 9 · 2021: 2 · 2020: 5 · 2019: 5 · 2018: 3
FWCI
1.45
Type
journal article
Language
en
Open access
Locations
  • Nature Communications (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • Ministry of Education, Culture, Sports, Science and Technology
  • Japan Society for the Promotion of Science (16K08580, 17K19615, 15K06994, 17K00548)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
Keywords
HBO1, histone acetyltransferase, phosphorylation, nucleotide excision repair, UV irradiation, cyclobutane pyrimidine dimers, XPC, SNF2H, chromatin remodeling, histone acetylation, xeroderma pigmentosum, ATM, ATR, DDB2, DNA damage response
MeSH terms
Bromodomain Containing Proteins, Adenosine Triphosphatases, Chromosomal Proteins, Non-Histone, DNA Damage, DNA Repair, DNA-Binding Proteins, Humans, Phosphorylation, Pyrimidine Dimers, Transcription Factors, Ultraviolet Rays, Histone Acetyltransferases, Ataxia Telangiectasia Mutated Proteins

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