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Lee, Ja Yil
School of Life Sciences
Research Interests
  • Investigated eukaryotic homologous recombination.

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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.author Cheon, Na Young ko
dc.contributor.author Kim, Hyun-Suk ko
dc.contributor.author Yeo, Jung-Eun ko
dc.contributor.author Scharer, Orlando D. ko
dc.contributor.author Lee, Ja Yil ko
dc.date.available 2019-09-02T09:03:58Z -
dc.date.created 2019-08-26 ko
dc.date.issued 2019-09 ko
dc.identifier.citation NUCLEIC ACIDS RESEARCH, v.47, no.16, pp.8337 - 8347 ko
dc.identifier.issn 0305-1048 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/27336 -
dc.description.abstract DNA 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. ko
dc.language 영어 ko
dc.publisher Oxford University Press ko
dc.title Single-molecule visualization reveals the damage search mechanism for the human NER protein XPC-RAD23B ko
dc.type ARTICLE ko
dc.identifier.wosid 000490576900007 ko
dc.type.rims ART ko
dc.identifier.doi 10.1093/nar/gkz629 ko
dc.identifier.url https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkz629/5542879 ko
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