• DOI:10.1103/PHYSREVLETT.95.208101
Corpus ID: 37405026

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

@article{Skoko2005LowforceDC,
  title={Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein Fis.},
  author={Dunja Skoko and J. Yan and R. Johnson and J. Marko},
  journal={Physical review letters},
  year={2005},
  volume={95 20},
  pages={
          208101
        }
}

Dunja Skoko, J. Yan, +1 author J. Marko

Published 2005

Chemistry, Medicine

Physical review letters

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… CONTINUE READING

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