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  1. 原著論文

Histone deacetylation regulates nucleotide excision repair through an interaction with the XPC protein

https://repo.qst.go.jp/records/85863
https://repo.qst.go.jp/records/85863
7ee1972c-9e33-47af-a43c-879ee5b3057f
Item type 学術雑誌論文 / Journal Article(1)
公開日 2022-04-05
タイトル
タイトル Histone deacetylation regulates nucleotide excision repair through an interaction with the XPC protein
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
アクセス権
アクセス権 metadata only access
アクセス権URI http://purl.org/coar/access_right/c_14cb
著者 Kusakabe, Masayuki

× Kusakabe, Masayuki

WEKO 1042743

Kusakabe, Masayuki

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Kakumu, Erina

× Kakumu, Erina

WEKO 1042744

Kakumu, Erina

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Kurihara, Fumika

× Kurihara, Fumika

WEKO 1042745

Kurihara, Fumika

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Tsuchida, Kazuki

× Tsuchida, Kazuki

WEKO 1042746

Tsuchida, Kazuki

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Maeda, Takumi

× Maeda, Takumi

WEKO 1042747

Maeda, Takumi

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Tada, Haruto

× Tada, Haruto

WEKO 1042748

Tada, Haruto

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Kusao, Kanako

× Kusao, Kanako

WEKO 1042749

Kusao, Kanako

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Kato, Akari

× Kato, Akari

WEKO 1042750

Kato, Akari

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Takeshi, Yasuda

× Takeshi, Yasuda

WEKO 1042751

Takeshi, Yasuda

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Matsuda, Tomonari

× Matsuda, Tomonari

WEKO 1042752

Matsuda, Tomonari

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Nakao, Mitsuyoshi

× Nakao, Mitsuyoshi

WEKO 1042753

Nakao, Mitsuyoshi

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Yokoi, Masayuki

× Yokoi, Masayuki

WEKO 1042754

Yokoi, Masayuki

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Sakai, Wataru

× Sakai, Wataru

WEKO 1042755

Sakai, Wataru

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Sugasawa, Kaoru

× Sugasawa, Kaoru

WEKO 1042756

Sugasawa, Kaoru

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Takeshi, Yasuda

× Takeshi, Yasuda

WEKO 1042757

en Takeshi, Yasuda

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抄録
内容記述タイプ Abstract
内容記述 The XPC protein complex plays a central role in DNA lesion recognition for global genome nucleotide excision repair (GG-NER). Lesion recognition can be accomplished in either a UV-DDB-dependent or -independent manner; however, it is unclear how these sub-pathways are regulated in chromatin. Here, we show that histone deacetylases 1 and 2 facilitate UV-DDB-independent recruitment of XPC to DNA damage by inducing histone deacetylation. XPC localizes to hypoacetylated chromatin domains in a DNA damage-independent manner, mediated by its structurally disordered middle (M) region. TheMregion interacts directly with the N-terminal tail of histone H3, an interaction compromised by H3 acetylation. Although the M region is dispensable for in vitro NER, it promotes DNA damage removal by GG-NER in vivo, particularly in the absence of UV-DDB. We propose that histone deacetylation around DNA damage facilitates the recruitment of XPC through the M region, contributing to efficient lesion recognition and initiation of GG-NER.
書誌情報 iScience

巻 25, 号 14, p. 104040, 発行日 2022-04
出版者
出版者 Cell Press
ISSN
収録物識別子タイプ ISSN
収録物識別子 2589-0042
DOI
識別子タイプ DOI
関連識別子 10.1016/j.isci.2022.104040
関連サイト
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.isci.2022.104040
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