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Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fis

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Title: Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fis
Author(s): Skoko, Dunja; Yan, Jie; Johnson, Reid C.; Marko, John F.
Subject(s): escherichia-coli stretching dna binding chromosome
Abstract: We 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.
Issue Date: 2005-11-11
Publisher: American Physical Society
Citation Info: Skoko, 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/e208101
Type: Article
Description: Publisher's Copyright: http://forms.aps.org/author/copytrnsfr.pdf
URI: http://hdl.handle.net/10027/6208
ISSN: 0031-9007
Date Available in INDIGO: 2009-08-08
 

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