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The interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain

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dc.contributor.authorPhuong Thi Mai Duong-
dc.contributor.authorAnh Thi Ngoc Bui-
dc.contributor.authorSeong-Ok Kim-
dc.contributor.authorHee-Sung Park-
dc.contributor.authorYeon-Soo Seo-
dc.contributor.authorByong-Seok Choi-
dc.date.accessioned2020-12-22T03:02:20Z-
dc.date.accessioned2020-12-22T03:02:20Z-
dc.date.available2020-12-22T03:02:20Z-
dc.date.available2020-12-22T03:02:20Z-
dc.date.created2020-06-12-
dc.date.issued2020-06-
dc.identifier.issn0014-5793-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/7848-
dc.description.abstract© 2020 Federation of European Biochemical Societies. Polymerase η (Polη) is one of the Y-family polymerases that is recruited by monoubiquitinated proliferating cell nuclear antigen (Ub-PCNA) to DNA damage sites during translesion synthesis (TLS). This interaction is mediated by an ubiquitin-binding zinc-finger (UBZ) domain and a PCNA-interacting protein (PIP) box in Polη, which binds to ubiquitin and PCNA, respectively. Here, we show that without the UBZ domain, the PIP box of yeast Polη has a novel binding function with ubiquitin. Furthermore, the UBZ domain and the PIP box share the same binding surfaces for ubiquitin. The interaction with ubiquitin via the PIP box stabilizes the Ub-PCNA/Polη complex. Moreover, the PIP residues I624 and L625 contribute to Polη function in TLS in vivo-
dc.language영어-
dc.publisherELSEVIER SCIENCE BV-
dc.subjectmonoubiquitinated PCNA-
dc.subjectpolymerase η-
dc.subjecttranslesion synthesis-
dc.subjectubiquitin-binding-
dc.subjectUBZ-
dc.titleThe interaction between ubiquitin and yeast polymerase η C terminus does not require the UBZ domain-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000538615100008-
dc.identifier.scopusid2-s2.0-85083102739-
dc.identifier.rimsid71982-
dc.contributor.affiliatedAuthorSeong-Ok Kim-
dc.identifier.doi10.1002/1873-3468.13783-
dc.identifier.bibliographicCitationFEBS LETTERS, v.594, no.11, pp.1726 - 1737-
dc.relation.isPartOfFEBS LETTERS-
dc.citation.titleFEBS LETTERS-
dc.citation.volume594-
dc.citation.number11-
dc.citation.startPage1726-
dc.citation.endPage1737-
dc.description.journalClass1-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordAuthormonoubiquitinated PCNA-
dc.subject.keywordAuthorpolymerase η-
dc.subject.keywordAuthortranslesion synthesis-
dc.subject.keywordAuthorubiquitin-binding-
dc.subject.keywordAuthorUBZ-
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HiddenCommunity > 1. Journal Papers (저널논문)
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