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  1. 原著論文

Role of the ubiquitin-binding domain of PolH in RaD 18-independent translesion DNA synthesis in human cell extracts

https://repo.qst.go.jp/records/46014
https://repo.qst.go.jp/records/46014
e7dd64c0-68a0-46eb-bc20-c44aa1afc4a1
Item type 学術雑誌論文 / Journal Article(1)
公開日 2011-03-08
タイトル
タイトル Role of the ubiquitin-binding domain of PolH in RaD 18-independent translesion DNA synthesis in human cell extracts
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 Schmutz, Valerie

× Schmutz, Valerie

WEKO 457946

Schmutz, Valerie

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Janel-Bintz, Regine

× Janel-Bintz, Regine

WEKO 457947

Janel-Bintz, Regine

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Wagner, Jerome

× Wagner, Jerome

WEKO 457948

Wagner, Jerome

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Biard, Denis

× Biard, Denis

WEKO 457949

Biard, Denis

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Shiomi, Naoko

× Shiomi, Naoko

WEKO 457950

Shiomi, Naoko

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P., Fuchs Robert

× P., Fuchs Robert

WEKO 457951

P., Fuchs Robert

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M., Cordonnier Agnes

× M., Cordonnier Agnes

WEKO 457952

M., Cordonnier Agnes

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塩見 尚子

× 塩見 尚子

WEKO 457953

en 塩見 尚子

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内容記述タイプ Abstract
内容記述 In eukaryotic cells, the Rad6/Rad18-dependent monoubiquitination of the proliferating cell nuclear antigen (PCNA) plays an essential role in the switching between replicatin and translesion DNA synthesis (TLS).The DNA polymerase PolHbinds to PCNA via a consensus C-terminal PCNA-interacting protein ( PIP) motif. It also specifically interacts with monoubiquitinated PCNA thanks to a recently identified ubiquitin-binding domain (UBZ).To investigate whether the TLS activity of PolHis always coupled to PCNA monoubiquitination, we monitor the ability of cell-free extracts to perform DNA synthesis across different types of lesions. We observe that a cis-syncyclobutane thymine dimer (TT-CPD),but not a N-2-2acetylaminouorene-guanine (G-AAF) adduct, is efficiently bypassed in extracts from Rad18-deficient cells, thus demonstrating the existence of a PolH -dependent and Rad18-independent TLS pathway .In addition ,by complementing PolH -deficient cells with PIP and UBZ mutants, we show that each of these domains contributes to PolH activity. The finding that the bypass of a CPD lesion in vitro does not require Ub-PCNA but nevertheless depends on the UBZ domain of PolH, reveals that this domain may play a novel role in the TLS process that is not related to the monoubiquitination status of PCNA.
書誌情報 Nucleic Acids Research

巻 38, 号 19, p. 6456-6465, 発行日 2010-06
ISSN
収録物識別子タイプ ISSN
収録物識別子 0305-1048
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