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

Please use this identifier to cite or link to this item: https://doi.org/10.1103/PhysRevLett.95.208101

Title:	Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein fis
Authors:	Skoko, D. Yan, J. Johnson, R.C. Marko, J.F.
Issue Date:	11-Nov-2005
Citation:	Skoko, D., Yan, J., Johnson, R.C., Marko, J.F. (2005-11-11). Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein fis. Physical Review Letters 95 (20) : -. ScholarBank@NUS Repository. https://doi.org/10.1103/PhysRevLett.95.208101
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*
Source Title:	Physical Review Letters
URI:	http://scholarbank.nus.edu.sg/handle/10635/97106
ISSN:	00319007
DOI:	10.1103/PhysRevLett.95.208101
Appears in Collections:	Staff Publications

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