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 Jie Yan and Reid C. Johnson and John F. Marko},
  journal={Physical review letters},
  year={2005},
  volume={95 20},
  pages={
          208101
        }
}
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… 
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Mechanism of chromosome compaction and looping by the Escherichia coli nucleoid protein Fis.

Mechanism of chromosome compaction and looping by the E. coli nucleoid protein Fis

Results suggest that Fis may play a role in vivo as a ‘domain barrier element’ by organizing DNA loops within the E. coli chromosome through Fis-mediated DNA looping.

Force-driven unbinding of proteins HU and Fis from DNA quantified using a thermodynamic Maxwell relation

Determining numbers of proteins bound to large DNAs is important for understanding their chromosomal functions. Protein numbers may be affected by physical factors such as mechanical forces generated…

Mechanisms of DNA Organization Unraveled with Novel Single-Molecule Methods

A setup with four independently moveable optical traps, enabling to manipulate two DNA molecules held between beads, shows that friction between the two polymers remains below 1 pN, and opens a wide range of experiments on proteins interacting with multiple DNA regions.

Structural change of DNA induced by nucleoid proteins: growth phase-specific Fis and stationary phase-specific Dps.

Interplay between the bacterial nucleoid protein H-NS and macromolecular crowding in compacting DNA

H-NS alone does not have a dramatic effect on DNA coil sizes in solution, but it does have an interesting synergetic effect on polymer-induced condensation of DNA, which suggests that protein-protein interactions have a much larger effect on H-NS self-association in solution than on the DNA binding properties.

Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA

Using single-DNA stretching and fluorescence detection, it is found that sequence-neutral DNA-binding proteins Fis, HU and NHP6A readily exchange with themselves and with each other, and solvated proteins can play a key role in facilitating removal and renewal of proteins bound to the double helix.

The architectural role of nucleoid-associated proteins in the organization of bacterial chromatin: a molecular perspective.

Multiple-binding-site mechanism explains concentration-dependent unbinding rates of DNA-binding proteins

This work uses a combination of coarse-grained simulation and theory to demonstrate that concentration-dependent unbinding rates of proteins from DNA can be explained by taking into account the dimeric nature of the protein, which permits partial dissociation and exchange with other proteins in solution.

Specific and non-specific interactions of ParB with DNA: implications for chromosome segregation

The experiments provide no evidence for the promotion of non-specific DNA binding and/or condensation events by the presence of parS sequences, and the implications for chromosome segregation are discussed.
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