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dc.contributor.authorNorthall, Sarah J
dc.contributor.authorBuckley, Ryan
dc.contributor.authorJones, Nathan
dc.contributor.authorPenedo-Esteiro, Juan Carlos
dc.contributor.authorSoultanas, Panos
dc.contributor.authorBolt, Edward
dc.date.accessioned2018-07-16T23:34:34Z
dc.date.available2018-07-16T23:34:34Z
dc.date.issued2017-09
dc.identifier.citationNorthall , S J , Buckley , R , Jones , N , Penedo-Esteiro , J C , Soultanas , P & Bolt , E 2017 , ' DNA binding and unwinding by Hel308 helicase requires dual functions of a winged helix domain ' , DNA Repair , vol. 57 , pp. 125-132 . https://doi.org/10.1016/j.dnarep.2017.07.005en
dc.identifier.issn1568-7864
dc.identifier.otherPURE: 250545388
dc.identifier.otherPURE UUID: e16699c4-0b78-404f-96ed-c5f1cfb96f0a
dc.identifier.otherScopus: 85025095832
dc.identifier.otherWOS: 000411535400015
dc.identifier.otherORCID: /0000-0002-5807-5385/work/74872780
dc.identifier.urihttp://hdl.handle.net/10023/15453
dc.description.abstractHel308 helicases promote genome stability linked to DNA replication in archaea, and have homologues in metazoans. In the crystal structure of archaeal Hel308 bound to a tailed DNA duplex, core helicase domains encircle single-stranded DNA (ssDNA) in a “ratchet” for directional translocation. A winged helix domain (WHD) is also present, but its function is mysterious. We investigated the WHD in full-length Hel308, identifying that mutations in a solvent exposed α-helix resulted in reduced DNA binding and unwinding activities. When isolated from the rest of Hel308, the WHD protein alone bound to duplex DNA but not ssDNA, and DNA binding by WHD protein was abolished by the same mutations as were analyzed in full-length Hel308. Isolated WHD from a human Hel308 homologue (HelQ) also bound to duplex DNA. By disrupting the interface between the Hel308 WHD and a RecA-like domain, a topology typical of Ski2 helicases, we show that this is crucial for ATPase and helicase activities. The data suggest a model in which the WHD promotes activity of Hel308 directly, through binding to duplex DNA that is distinct from ssDNA binding by core helicase, and indirectly through interaction with the RecA-like domain. We propose how the WHD may contribute to ssDNA translocation, resulting in DNA helicase activity or in removal of other DNA bound proteins by “reeling” ssDNA.
dc.format.extent7
dc.language.isoeng
dc.relation.ispartofDNA Repairen
dc.rights© 2017, Elsevier. This work has been made available online in accordance with the publisher’s policies. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version. The final published version of this work is available at www.sciencedirect.com / https://doi.org/10.1016/j.dnarep.2017.07.005en
dc.subjectHelicaseen
dc.subjectDNA repairen
dc.subjectHomologous recombinationen
dc.subjectArchaeaen
dc.subjectHelQen
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectNDASen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.titleDNA binding and unwinding by Hel308 helicase requires dual functions of a winged helix domainen
dc.typeJournal articleen
dc.description.versionPostprinten
dc.contributor.institutionUniversity of St Andrews. School of Physics and Astronomyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1016/j.dnarep.2017.07.005
dc.description.statusPeer revieweden
dc.date.embargoedUntil2018-07-16


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