DSpace at EWHA: XPC-RAD23B enhances UV-DDB binding to DNA to facilitate lesion search in nucleotide excision repair

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DC Field	Value	Language
dc.contributor.author	장선복	*
dc.date.accessioned	2025-10-29T16:31:08Z	-
dc.date.available	2025-10-29T16:31:08Z	-
dc.date.issued	2025	*
dc.identifier.issn	1362-4962	*
dc.identifier.other	OAK-38064	*
dc.identifier.uri	https://dspace.ewha.ac.kr/handle/2015.oak/273201	-
dc.description.abstract	Ultraviolet-induced DNA lesions are removed by the nucleotide excision repair (NER) pathway. In global-genome NER (GG-NER), XPC-RAD23B recognizes the lesions and initiates NER. However, cyclobutane pyrimidine dimers (CPDs), which do not significantly destabilize the DNA duplex, are not bound by XPC-RAD23B with high selectivity. Instead, CPD is preferentially sensed by UV-DDB, which is believed to hand over the lesion to XPC-RAD23B via ubiquitination of both proteins. Here, by combining biochemical and single-molecule DNA curtain assays, we investigate the interactions between UV-DDB and XPC-RAD23B on DNA. Surprisingly, we discover that XPC-RAD23B enhances the binding of UV-DDB to DNA. We demonstrate that this enhancement can be attributed to the complex formation of UV-DDB and XPC-RAD23B (UX-complex), which increases the binding affinity of UV-DDB to undamaged DNA. We further show that UV-DDB finds CPDs through one-dimensional (1D) diffusion along DNA. Collectively, the UX-complex enhances UV-DDB loading to DNA to accelerate the search for CPD via 1D diffusion. Moreover, we find that UV-DDB and XPC-RAD23B can bind CPDs as a complex, which facilitates the transfer of CPD. Altogether, our results show that UV-DDB and XPC-RAD23B cooperatively interact for rapid CPD search, providing a new mechanism for lesion search in GG-NER. © 2025 Elsevier B.V., All rights reserved.	*
dc.language	English	*
dc.publisher	Oxford University Press	*
dc.subject	Dna	*
dc.subject	Dna Ligase	*
dc.subject	Pyrimidine Dimer	*
dc.subject	Dna Repair Enzymes	*
dc.subject	Dna-binding Proteins	*
dc.subject	Pyrimidine Dimers	*
dc.subject	Rad23b Protein, Human	*
dc.subject	Xpc Protein, Human	*
dc.subject	Dna Binding Protein	*
dc.subject	Protein Binding	*
dc.subject	Article	*
dc.subject	Assay	*
dc.subject	Binding Affinity	*
dc.subject	Blotting	*
dc.subject	Controlled Study	*
dc.subject	Diffusion	*
dc.subject	Dna Binding	*
dc.subject	Dna Damage	*
dc.subject	Dna Repair	*
dc.subject	Fluorescence Imaging	*
dc.subject	Fluorescence Recovery After Photobleaching	*
dc.subject	Gel Filtration Chromatography	*
dc.subject	Gel Mobility Shift Assay	*
dc.subject	Human	*
dc.subject	Immunoprecipitation	*
dc.subject	In Vitro Study	*
dc.subject	Native Gel Western Blot	*
dc.subject	Nonhuman	*
dc.subject	Nucleotide Excision Repair	*
dc.subject	Polyacrylamide Gel Electrophoresis	*
dc.subject	Protein Interaction	*
dc.subject	Protein Purification	*
dc.subject	Protein Structure	*
dc.subject	Pull-down Assay	*
dc.subject	Single Molecule Dna Curtain Assay	*
dc.subject	Surface Plasmon Resonance	*
dc.subject	Ultraviolet Radiation	*
dc.subject	Western Blotting	*
dc.subject	Chemistry	*
dc.subject	Excision Repair	*
dc.subject	Genetics	*
dc.subject	Metabolism	*
dc.subject	Humans	*
dc.subject	Ultraviolet Rays	*
dc.title	XPC-RAD23B enhances UV-DDB binding to DNA to facilitate lesion search in nucleotide excision repair	*
dc.type	Article	*
dc.relation.issue	11	*
dc.relation.volume	53	*
dc.relation.index	SCIE	*
dc.relation.index	SCOPUS	*
dc.relation.journaltitle	Nucleic Acids Research	*
dc.identifier.doi	10.1093/nar/gkaf463	*
dc.identifier.wosid	WOS:001518025900001	*
dc.identifier.scopusid	2-s2.0-105008993067	*
dc.author.google	An S.	*
dc.author.google	Kusakabe M.	*
dc.author.google	Kim H.	*
dc.author.google	Kozono H.	*
dc.author.google	Cheon N.	*
dc.author.google	Kim J.	*
dc.author.google	Kang J.	*
dc.author.google	Jang S.	*
dc.author.google	Sugasawa K.	*
dc.author.google	Schärer O.D.	*
dc.contributor.scopusid	장선복(23389133200)	*
dc.date.modifydate	20260813141434	*