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This homotetrameric protein wraps ssDNA in multiple distinct binding modes that may be used selectively in different DNA processes, and whose detailed wrapping topologies remain speculative. Here, we used single-molecule force and fluorescence spectroscopy to investigate E. coli SSB binding to ssDNA. Stretching a single ssDNA-SSB complex reveals discrete states that correlate with known binding modes, the likely ssDNA conformations and diffusion dynamics in each, and the kinetic pathways by which the protein wraps ssDNA and is dissociated. The data allow us to construct an energy landscape for the ssDNA-SSB complex, revealing that unwrapping energy costs increase the more ssDNA is unraveled. Our findings provide insights into the mechanism by which proteins gain access to ssDNA bound by SSB, as demonstrated by experiments in which SSB is displaced by the E. coli recombinase RecA.<\/jats:p>","DOI":"10.7554\/elife.08193","type":"journal-article","created":{"date-parts":[[2015,8,25]],"date-time":"2015-08-25T07:31:51Z","timestamp":1440487911000},"source":"Crossref","is-referenced-by-count":95,"title":["Structural dynamics of E. coli single-stranded DNA binding protein reveal DNA wrapping and unwrapping pathways"],"prefix":"10.7554","volume":"4","author":[{"given":"Sukrit","family":"Suksombat","sequence":"first","affiliation":[{"name":"Department of Physics, Center for the Physics of Living Cells, Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rustem","family":"Khafizov","sequence":"additional","affiliation":[{"name":"Department of Physics, Center for the Physics of Living Cells, Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander G","family":"Kozlov","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Timothy M","family":"Lohman","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yann R","family":"Chemla","sequence":"additional","affiliation":[{"name":"Department of Physics, Center for the Physics of Living Cells, Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, United States"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2015,8,25]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"6185","DOI":"10.1073\/pnas.94.12.6185","article-title":"Ionic effects on the elasticity of single DNA molecules","volume":"94","author":"Baumann","year":"1997","journal-title":"Proceedings of the National Academy of Sciences of USA"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"274","DOI":"10.1038\/nature11598","article-title":"Direct imaging of RecA nucleation and growth on single molecules of SSB-coated ssDNA","volume":"491","author":"Bell","year":"2012","journal-title":"Nature"},{"key":"bib3","doi-asserted-by":"publisher","first-page":"1373","DOI":"10.1073\/pnas.1318001111","article-title":"Structural mechanisms of PriA-mediated DNA replication restart","volume":"111","author":"Bhattacharyya","year":"2014","journal-title":"Proceedings of the National Academy of Sciences of USA"},{"key":"bib4","doi-asserted-by":"publisher","first-page":"517","DOI":"10.1038\/nmeth.1217","article-title":"Laminar flow cells for single-molecule studies of DNA-protein interactions","volume":"5","author":"Brewer","year":"2008","journal-title":"Nature Methods"},{"key":"bib5","doi-asserted-by":"publisher","first-page":"7799","DOI":"10.1021\/bi00372a003","article-title":"Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA","volume":"25","author":"Bujalowski","year":"1986","journal-title":"Biochemistry"},{"key":"bib7","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1016\/0022-2836(89)90454-3","article-title":"Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. 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