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dc.contributor.authorSkoko, Dunja
dc.contributor.authorYan, Jie
dc.contributor.authorJohnson, Reid C.
dc.contributor.authorMarko, John F.
dc.date.accessioned2009-08-08T16:33:47Z
dc.date.available2009-08-08T16:33:47Z
dc.date.issued2005-11-11
dc.identifier.bibliographicCitationSkoko, D., Yan, J., Johnson, R. C., & Marko, J. F. (2005). Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fis. Physical Review Letters, 95. http://link.aps.org/abstract/PRL/v95/e208101en
dc.identifier.issn0031-9007
dc.identifier.otherDOI: 10.1103/PhysRevLett.95.208101
dc.identifier.urihttp://hdl.handle.net/10027/6208
dc.descriptionPublisher's Copyright: http://forms.aps.org/author/copytrnsfr.pdfen
dc.description.abstractWe report single-DNA-stretching experiments showing that the protein Fis, an abundant bacterial chromosome protein of E. coli, mediates a dramatic DNA condensation to zero length. This condensation occurs abruptly when DNA tension is reduced below a protein-concentration-dependent threshold f(*)< 1 pN. Following condensation, reopening under larger forces proceeds via a series of discrete jumps, indicating that Fis is able to stabilize DNA crossings. Our experiments suggest that Fis may play a role in vivo stabilizing the "loop-domain" structure of the bacterial chromosome.en
dc.publisherAmerican Physical Societyen
dc.subjectescherichia-colien
dc.subjectstretching dnaen
dc.subjectbindingen
dc.subjectchromosomeen
dc.titleLow-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fisen
dc.typeArticleen


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