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Please use this identifier to cite or link to this item:
http://hdl.handle.net/10027/6208
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| Title: | Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fis |
| Authors: | Skoko, Dunja
Yan, Jie
Johnson, Reid C.
Marko, John F. |
| Keywords: | escherichia-coli
stretching dna
binding
chromosome |
| Issue Date: | 11-Nov-2005 |
| Publisher: | American Physical Society |
| Citation: | 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 |
| 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. |
| Description: | Publisher's Copyright: http://forms.aps.org/author/copytrnsfr.pdf |
| URI: | http://hdl.handle.net/10027/6208 |
| ISSN: | 0031-9007 |
| Appears in Collections: | Publications - Physics
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Files in This Item:
| File |
Description |
Size | Format |
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| skoko low-force.pdf | | 228Kb | Adobe PDF | View/Open |
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