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dc.contributor.authorMorten, Michael John
dc.contributor.authorGamsjaeger, Roland
dc.contributor.authorCubeddu, Liza
dc.contributor.authorKariawasam, Ruvini
dc.contributor.authorPeregrina, Jose Ramon
dc.contributor.authorPenedo-Esteiro, Juan Carlos
dc.contributor.authorWhite, Malcolm Frederick
dc.date.accessioned2017-01-11T15:30:10Z
dc.date.available2017-01-11T15:30:10Z
dc.date.issued2017-03
dc.identifier.citationMorten , M J , Gamsjaeger , R , Cubeddu , L , Kariawasam , R , Peregrina , J R , Penedo-Esteiro , J C & White , M F 2017 , ' High-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding protein ' , Extremophiles , vol. 21 , no. 2 , pp. 369-379 . https://doi.org/10.1007/s00792-016-0910-2en
dc.identifier.issn1431-0651
dc.identifier.otherPURE: 248458033
dc.identifier.otherPURE UUID: 39a61058-9a03-4e85-8d3a-da42303f4952
dc.identifier.otherWOS: 000397971100012
dc.identifier.otherScopus: 85009179824
dc.identifier.otherWOS: 000397971100012
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136137
dc.identifier.otherORCID: /0000-0002-5807-5385/work/74872756
dc.identifier.urihttp://hdl.handle.net/10023/10082
dc.description.abstractSingle-stranded DNA-binding proteins (SSBs), including replication protein A (RPA) in eukaryotes, play a central role in DNA replication, recombination, and repair. SSBs utilise an oligonucleotide/oligosaccharide-binding (OB) fold domain to bind DNA, and typically oligomerise in solution to bring multiple OB fold domains together in the functional SSB. SSBs from hyperthermophilic crenarchaea, such as Sulfolobus solfataricus, have an unusual structure with a single OB fold coupled to a flexible C-terminal tail. The OB fold resembles those in RPA, whilst the tail is reminiscent of bacterial SSBs and mediates interaction with other proteins. One paradigm in the field is that SSBs bind specifically to ssDNA and much less strongly to RNA, ensuring that their functions are restricted to DNA metabolism. Here, we use a combination of biochemical and biophysical approaches to demonstrate that the binding properties of S. solfataricus SSB are essentially identical for ssDNA and ssRNA. These features may represent an adaptation to a hyperthermophilic lifestyle, where DNA and RNA damage is a more frequent event.
dc.format.extent11
dc.language.isoeng
dc.relation.ispartofExtremophilesen
dc.rights© The Author(s) 2017. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.en
dc.subjectRNA binding proteinsen
dc.subjectOB folden
dc.subjectSingle-molecule dynamicsen
dc.subjectFörster resonance energy transferen
dc.subjectNuclear magnetic resonanceen
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectQH426 Geneticsen
dc.subjectNDASen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.subject.lccQH426en
dc.titleHigh-affinity RNA binding by a hyperthermophilic single-stranded DNA-binding proteinen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
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/10.1007/s00792-016-0910-2
dc.description.statusPeer revieweden


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