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Binding dynamics of a monomeric SSB protein to DNA : a single-molecule multi-process approach
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dc.contributor.author | Morten, Michael John | |
dc.contributor.author | Peregrina, Jose Ramon | |
dc.contributor.author | Figueira-Gonzalez, Maria | |
dc.contributor.author | Ackermann, Katrin | |
dc.contributor.author | Bode, Bela Ernest | |
dc.contributor.author | White, Malcolm F | |
dc.contributor.author | Penedo, Carlos | |
dc.date.accessioned | 2015-11-23T14:40:10Z | |
dc.date.available | 2015-11-23T14:40:10Z | |
dc.date.issued | 2015-12-15 | |
dc.identifier | 229885552 | |
dc.identifier | aa7ed708-2794-41e0-8963-3d7583aa5c3e | |
dc.identifier | 84964608137 | |
dc.identifier | 000371237600036 | |
dc.identifier.citation | Morten , 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 . https://doi.org/10.1093/nar/gkv1225 | en |
dc.identifier.issn | 0305-1048 | |
dc.identifier.other | ORCID: /0000-0003-1543-9342/work/47136127 | |
dc.identifier.other | ORCID: /0000-0002-3384-271X/work/27582724 | |
dc.identifier.other | ORCID: /0000-0002-5807-5385/work/74872763 | |
dc.identifier.uri | https://hdl.handle.net/10023/7830 | |
dc.description | People 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.abstract | Single-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.format.extent | 18 | |
dc.format.extent | 6095919 | |
dc.language.iso | eng | |
dc.relation.ispartof | Nucleic Acids Research | en |
dc.subject | QC Physics | en |
dc.subject | QD Chemistry | en |
dc.subject | QR Microbiology | en |
dc.subject | NDAS | en |
dc.subject | BDC | en |
dc.subject | R2C | en |
dc.subject.lcc | QC | en |
dc.subject.lcc | QD | en |
dc.subject.lcc | QR | en |
dc.title | Binding dynamics of a monomeric SSB protein to DNA : a single-molecule multi-process approach | en |
dc.type | Journal article | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.sponsor | European Commission | en |
dc.contributor.sponsor | The Wellcome Trust | en |
dc.contributor.institution | University of St Andrews. School of Chemistry | en |
dc.contributor.institution | University of St Andrews. EaSTCHEM | en |
dc.contributor.institution | University of St Andrews. Biomedical Sciences Research Complex | en |
dc.contributor.institution | University of St Andrews. Centre of Magnetic Resonance | en |
dc.contributor.institution | University of St Andrews. School of Biology | en |
dc.contributor.institution | University of St Andrews. School of Physics and Astronomy | en |
dc.identifier.doi | 10.1093/nar/gkv1225 | |
dc.description.status | Peer reviewed | en |
dc.identifier.url | https://academic.oup.com/nar/article/43/22/10907/1804518#81924285 | en |
dc.identifier.grantnumber | 099149/Z/12/Z | en |
dc.identifier.grantnumber | en | |
dc.identifier.grantnumber | 091825/Z/10/Z | en |
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