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; Masatoshi Kitagawa

doi:10.1038/ncomms16102

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, Masatoshi Kitagawa

Research output: Contribution to journal › Article › peer-review

23 Citations (Scopus)

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.

Original language	English
Article number	16102
Journal	Nature communications
Volume	8
DOIs	https://doi.org/10.1038/ncomms16102
Publication status	Published - 2017 Jul 18
Externally published	Yes

ASJC Scopus subject areas

Chemistry(all)
Biochemistry, Genetics and Molecular Biology(all)
Physics and Astronomy(all)

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10.1038/ncomms16102

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title = "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.",

author = "Hiroyuki Niida and Ryoichi Matsunuma and Ryo Horiguchi and Chiharu Uchida and Yuka Nakazawa and Akira Motegi and Koji Nishimoto and Satoshi Sakai and Tatsuya Ohhata and Kyoko Kitagawa and Shinichi Moriwaki and Hideo Nishitani and Ayako Ui and Tomoo Ogi and Masatoshi Kitagawa",

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AU - Niida, Hiroyuki

AU - Matsunuma, Ryoichi

AU - Horiguchi, Ryo

AU - Uchida, Chiharu

AU - Nakazawa, Yuka

AU - Motegi, Akira

AU - Nishimoto, Koji

AU - Sakai, Satoshi

AU - Ohhata, Tatsuya

AU - Kitagawa, Kyoko

AU - Moriwaki, Shinichi

AU - Nishitani, Hideo

AU - Ui, Ayako

AU - Ogi, Tomoo

AU - Kitagawa, Masatoshi

PY - 2017/7/18

Y1 - 2017/7/18

N2 - 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.

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

Abstract

ASJC Scopus subject areas

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