Show simple item record

Files in this item


Item metadata

dc.contributor.authorRudolf, Jana
dc.contributor.authorRouillon, Christophe
dc.contributor.authorSchwarz-Linek, Ulrich
dc.contributor.authorWhite, Malcolm F
dc.identifier.citationRudolf , J , Rouillon , C , Schwarz-Linek , U & White , M F 2010 , ' The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway ' , Nucleic Acids Research , vol. 38 , no. 3 , pp. 931-941 .
dc.identifier.otherPURE: 1190481
dc.identifier.otherPURE UUID: 733d990e-9348-4ea1-801a-264a95687cdb
dc.identifier.otherWOS: 000274496900026
dc.identifier.otherScopus: 77950366206
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136128
dc.identifier.otherORCID: /0000-0003-0526-223X/work/40714977
dc.description.abstractXeroderma pigmentosum factor D (XPD) is a 5'-3' superfamily 2 helicase and the founding member of a family of DNA helicases with iron-sulphur cluster domains. As a component of transcription factor II H (TFIIH), XPD is involved in DNA unwinding during nucleotide excision repair (NER). Archaeal XPD is closely related in sequence to the eukaryal enzyme and the crystal structure of the archaeal enzyme has provided a molecular understanding of mutations causing xeroderma pigmentosum and trichothiodystrophy in humans. Consistent with a role in NER, we show that archaeal XPD can initiate unwinding from a DNA bubble structure, differentiating it from the related helicases FancJ and DinG. XPD was not stalled by substrates containing extrahelical fluorescein adducts, abasic sites nor a cyclobutane pyrimidine dimer, regardless of whether these modifications were placed on either the displaced or translocated strands. This suggests that DNA lesions repaired by NER may not present a barrier to XPD translocation in vivo, in contrast to some predictions. Preferential binding of a fluorescein-adducted oligonucleotide was observed, and XPD helicase activity was readily inhibited by both single- and double-stranded DNA binding proteins. These observations have several implications for the current understanding of the NER pathway.
dc.relation.ispartofNucleic Acids Researchen
dc.rights© The Author(s) 2009. Published by Oxford University Press. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectReplication protein-aen
dc.subjectRAD3 Proteinen
dc.subjectQH426 Geneticsen
dc.subjectSDG 3 - Good Health and Well-beingen
dc.titleThe helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathwayen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

This item appears in the following Collection(s)

Show simple item record