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유전체항상성연구단
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Single-molecule visualization reveals the damage search mechanism for the human NER protein XPC-RAD23B

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dc.contributor.authorNa Young Cheon-
dc.contributor.authorHyun-Suk Kim-
dc.contributor.authorJung-Eun Yeo-
dc.contributor.authorOrlando D Schärer-
dc.contributor.authorJa Yil Lee-
dc.date.available2019-10-11T08:06:55Z-
dc.date.created2019-09-18-
dc.date.issued2019-09-
dc.identifier.issn0305-1048-
dc.identifier.urihttps://pr.ibs.re.kr/handle/8788114/6272-
dc.description.abstractDNA repair is critical for maintaining genomic integrity. Finding DNA lesions initiates the entire repair process. In human nucleotide excision repair (NER), XPC-RAD23B recognizes DNA lesions and recruits downstream factors. Although previous studies revealed the molecular features of damage identification by the yeast orthologs Rad4-Rad23, the dynamic mechanisms by which human XPC-RAD23B recognizes DNA defects have remained elusive. Here, we directly visualized the motion of XPC-RAD23B on undamaged and lesion-containing DNA using high-throughput single-molecule imaging. We observed three types of one-dimensional motion of XPC-RAD23B along DNA: diffusive, immobile and constrained. We found that consecutive AT-tracks led to increase in proteins with constrained motion. The diffusion coefficient dramatically increased according to ionic strength, suggesting that XPC-RAD23B diffuses along DNA via hopping, allowing XPC-RAD23B to bypass protein obstacles during the search for DNA damage. We also examined how XPC-RAD23B identifies cyclobutane pyrimidine dimers (CPDs) during diffusion. XPC-RAD23B makes futile attempts to bind to CPDs, consistent with low CPD recognition efficiency. Moreover, XPC-RAD23B binds CPDs in biphasic states, stable for lesion recognition and transient for lesion interrogation. Taken together, our results provide new insight into how XPC-RAD23B searches for DNA lesions in billions of base pairs in human genome. C.The Author(s) 2019. Published by Oxford University Press on behalf of Nucleic Acids Research.-
dc.description.uri1-
dc.language영어-
dc.publisherOXFORD UNIV PRESS-
dc.titleSingle-molecule visualization reveals the damage search mechanism for the human NER protein XPC-RAD23B-
dc.typeArticle-
dc.type.rimsART-
dc.identifier.wosid000490576900007-
dc.identifier.scopusid2-s2.0-85073310181-
dc.identifier.rimsid69829-
dc.contributor.affiliatedAuthorHyun-Suk Kim-
dc.contributor.affiliatedAuthorJung-Eun Yeo-
dc.contributor.affiliatedAuthorOrlando D Schärer-
dc.contributor.affiliatedAuthorJa Yil Lee-
dc.identifier.doi10.1093/nar/gkz629-
dc.identifier.bibliographicCitationNUCLEIC ACIDS RESEARCH, v.47, no.16, pp.8337 - 8347-
dc.citation.titleNUCLEIC ACIDS RESEARCH-
dc.citation.volume47-
dc.citation.number16-
dc.citation.startPage8337-
dc.citation.endPage8347-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > 1. Journal Papers (저널논문)
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