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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/46014e7dd64c0-68a0-46eb-bc20-c44aa1afc4a1
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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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× Janel-Bintz, Regine× Wagner, Jerome× Biard, Denis× Shiomi, Naoko× P., Fuchs Robert× M., Cordonnier Agnes× 塩見 尚子 |
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抄録 | ||||||
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 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0305-1048 |