Dataset Information

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

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.

SUBMITTER: Niida H

PROVIDER: S-EPMC5520108 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

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

Niida Hiroyuki H Matsunuma Ryoichi R Horiguchi Ryo R Uchida Chiharu C Nakazawa Yuka Y Motegi Akira A Nishimoto Koji K Sakai Satoshi S Ohhata Tatsuya T Kitagawa Kyoko K Moriwaki Shinichi S Nishitani Hideo H Ui Ayako A Ogi Tomoo T Kitagawa Masatoshi M

Nature communications 20170718

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 ...[more]

PMID: 28719581

Dataset Information

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

Publications

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

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Similar Datasets

E2F1 localizes to sites of UV-induced DNA damage to enhance nucleotide excision repair.
| S-EPMC2885209 | biostudies-literature

UV radiation-induced SUMOylation of DDB2 regulates nucleotide excision repair.
| S-EPMC7446238 | biostudies-literature

Contributions of nucleotide excision repair, DNA polymerase eta, and homologous recombination to replication of UV-irradiated herpes simplex virus type 1.
| S-EPMC2859539 | biostudies-literature

ABF1-binding sites promote efficient global genome nucleotide excision repair.
| S-EPMC3443742 | biostudies-literature

Influence of XPB helicase on recruitment and redistribution of nucleotide excision repair proteins at sites of UV-induced DNA damage.
| S-EPMC3471374 | biostudies-literature

The mechanism of nucleotide excision repair-mediated UV-induced mutagenesis in nonproliferating cells.
| S-EPMC3583999 | biostudies-literature

Prokaryotic nucleotide excision repair.
| S-EPMC3578354 | biostudies-literature

The AHR represses nucleotide excision repair and apoptosis and contributes to UV-induced skin carcinogenesis.
| S-EPMC6180092 | biostudies-literature

UV wavelength-dependent regulation of transcription-coupled nucleotide excision repair in p53-deficient human cells.
| S-EPMC165856 | biostudies-literature

Regulation of nucleotide excision repair by UV-DDB: prioritization of damage recognition to internucleosomal DNA.
| S-EPMC3201922 | biostudies-literature