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  1. 原著論文

Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3

https://repo.qst.go.jp/records/47888
https://repo.qst.go.jp/records/47888
f1bed5e7-be93-4758-b510-f399b8122ded
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-04-27
タイトル
タイトル Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3
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 Kakumu, Erina

× Kakumu, Erina

WEKO 480750

Kakumu, Erina

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Nakanishi, Seiya

× Nakanishi, Seiya

WEKO 480751

Nakanishi, Seiya

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M., Shiratori Hiromi

× M., Shiratori Hiromi

WEKO 480752

M., Shiratori Hiromi

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Kato, Akari

× Kato, Akari

WEKO 480753

Kato, Akari

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Kobayashi, Wataru

× Kobayashi, Wataru

WEKO 480754

Kobayashi, Wataru

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Machida, Shinichi

× Machida, Shinichi

WEKO 480755

Machida, Shinichi

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Yasuda, Takeshi

× Yasuda, Takeshi

WEKO 480756

Yasuda, Takeshi

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Adachi, Naoko

× Adachi, Naoko

WEKO 480757

Adachi, Naoko

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Saito, Naoaki

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WEKO 480758

Saito, Naoaki

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Ikura, Tsuyoshi

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WEKO 480759

Ikura, Tsuyoshi

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Kurumizaka, Hitoshi

× Kurumizaka, Hitoshi

WEKO 480760

Kurumizaka, Hitoshi

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Kimura, Hiroshi

× Kimura, Hiroshi

WEKO 480761

Kimura, Hiroshi

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Yokoi, Masayuki

× Yokoi, Masayuki

WEKO 480762

Yokoi, Masayuki

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Sakai, Wataru

× Sakai, Wataru

WEKO 480763

Sakai, Wataru

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Sugasawa, Kaoru

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WEKO 480764

Sugasawa, Kaoru

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安田 武嗣

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WEKO 480765

en 安田 武嗣

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抄録
内容記述タイプ Abstract
内容記述 In the mammalian global genome nucleotide excision repair pathway, two damage recognition factors, XPC and UV-DDB, play pivotal roles in the initiation of the repair reaction. However, the molecular mechanisms underlying regulation of the lesion recognition process in the context of chromatin structures remain to be understood. Here, we show evidence that damage recognition factors tend to associate with chromatin regions devoid of certain types of acetylated histones. Treatment of cells with histone deacetylase inhibitors retarded recruitment of XPC to sites of UV-induced DNA damage and the subsequent repair process. Biochemical studies showed novel multifaceted interactions of XPC with histone H3, which were profoundly impaired by deletion of the N-terminal tail of histone H3. In addition, histone H1 also interacted with XPC. Importantly, acetylation of histone H3 markedly attenuated the interaction with XPC in vitro, and local UV irradiation of cells decreased the level of H3K27ac in the damaged areas. Our results suggest that histone deacetylation plays a significant role in the process of DNA damage recognition for nucleotide excision repair and that the localization and functions of XPC can be regulated by acetylated states of histones.
書誌情報 Genes to Cells

巻 22, 号 3, p. 310-327, 発行日 2017-03
出版者
出版者 Wiley-Japan
DOI
識別子タイプ DOI
関連識別子 10.1111/gtc.12479
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