期刊
NUCLEIC ACIDS RESEARCH
卷 43, 期 22, 页码 -出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv1225
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资金
- People Programme of the European Union's Seventh Framework Programme [REA 334496]
- Leonardo da Vinci European Union Programme
- Wellcome Trust [099149/Z/12/Z, 091825/Z/10/Z]
- Wellcome Trust
- University of St Andrews
- Biotechnology and Biological Sciences Research Council [1100198] Funding Source: researchfish
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 Forster 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 high-density 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.
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