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dc.contributor.authorMorten, Michael John
dc.contributor.authorPeregrina, Jose Ramon
dc.contributor.authorFigueira-Gonzalez, Maria
dc.contributor.authorAckermann, Katrin
dc.contributor.authorBode, Bela Ernest
dc.contributor.authorWhite, Malcolm F
dc.contributor.authorPenedo, Carlos
dc.identifier.citationMorten , M J , Peregrina , J R , Figueira-Gonzalez , M , Ackermann , K , Bode , B E , White , M F & Penedo , C 2015 , ' Binding dynamics of a monomeric SSB protein to DNA : a single-molecule multi-process approach ' , Nucleic Acids Research , vol. 43 , no. 22 , pp. 10907-10924 .
dc.identifier.otherPURE: 229885552
dc.identifier.otherPURE UUID: aa7ed708-2794-41e0-8963-3d7583aa5c3e
dc.identifier.otherScopus: 84964608137
dc.identifier.otherORCID: /0000-0003-1543-9342/work/47136127
dc.identifier.otherORCID: /0000-0002-3384-271X/work/27582724
dc.identifier.otherWOS: 000371237600036
dc.identifier.otherORCID: /0000-0002-5807-5385/work/74872763
dc.descriptionPeople Programme of the European Union’s Seventh Framework Programme [REA 334496 to B.E.B.]; Leonardo da Vinci European Union Programme (to M.F.G.); Wellcome Trust [099149/Z/12/Z, 091825/Z/10/Z]. Funding for open access charge: Wellcome Trust; University of St Andrews.en
dc.description.abstractSingle-stranded DNA binding proteins (SSBs) are ubiquitous across all organisms and are characterized by the presence of an OB (oligonucleotide/oligosaccharide/oligopeptide) binding motif to recognize single-stranded DNA (ssDNA). Despite their critical role in genome maintenance, our knowledge about SSB function is limited to proteins containing multiple OB-domains and little is known about single OB-folds interacting with ssDNA. Sulfolobus solfataricus SSB (SsoSSB) contains a single OB-fold and being the simplest representative of the SSB-family may serve as a model to understand fundamental aspects of SSB:DNA interactions. Here, we introduce a novel approach based on the competition between Förster resonance energy transfer (FRET), protein-induced fluorescence enhancement (PIFE) and quenching to dissect SsoSSB binding dynamics at single monomer resolution. We demonstrate that SsoSSB follows a monomer-by-monomer binding mechanism that involves a positive-cooperativity component between adjacent monomers. We found that SsoSSB dynamic behaviour is closer to that of Replication Protein A than to Escherichia coli SSB; a feature that might be inherited from the structural analogies of their DNA-binding domains. We hypothesize that SsoSSB has developed a balance between highdensity binding and a highly dynamic interaction with ssDNA to ensure efficient protection of the genome but still allow access to ssDNA during vital cellular processes.
dc.relation.ispartofNucleic Acids Researchen
dc.rights© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectQC Physicsen
dc.subjectQD Chemistryen
dc.subjectQR Microbiologyen
dc.titleBinding dynamics of a monomeric SSB protein to DNA : a single-molecule multi-process approachen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.sponsorEuropean Commissionen
dc.contributor.sponsorThe Wellcome Trusten
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. Centre of Magnetic Resonanceen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. School of Physics and Astronomyen
dc.description.statusPeer revieweden

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