Abstract
Recent work has demonstrated concentrationdependent unbinding rates of proteins from DNA, using fluorescence visualization of the bacterial nucleoid protein Fis [Graham et al. (2011) (Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA. Nucleic Acids Res., 39:2249)]. The physical origin of this concentration-dependence is unexplained. We use a combination of coarse-grained simulation and theory to demonstrate that this behavior can be explained by taking into account the dimeric nature of the protein, which permits partial dissociation and exchange with other proteins in solution. Concentration-dependent unbinding is generated by this simple model, quantitatively explaining experimental data. This effect is likely to play a major role in determining binding lifetimes of proteins in vivo where there are very high concentrations of solvated molecules.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3783-3791 |
| Number of pages | 9 |
| Journal | Nucleic acids research |
| Volume | 42 |
| Issue number | 6 |
| DOIs | |
| State | Published - Apr 2014 |
Funding
National Science Foundation [DMR-0907781, MCB-1022117 and DMR-1206868]; the National Institutes of Health [1U54CA143869-01 (NU-PS-OC) and 1R01GM105847-01]; the Office of the Director of Defense Research and Engineering and Air Force Office of Scientific Research [FA9550-10-1-0167]; and the Northwestern International Institute for Nanotechnology. Funding for open access charge: NIH [1U54CA143869-01].
ASJC Scopus subject areas
- Genetics