Preferential binding of the archaebacterial histone-like MC1 protein to negatively supercoiled DNA minicircles.

@article{Teyssier1996PreferentialBO,
  title={Preferential binding of the archaebacterial histone-like MC1 protein to negatively supercoiled DNA minicircles.},
  author={C Teyssier and Francine Toulm{\'e} and J. Touzel and Alain L. Gervais and Jean Claude Maurizot and Françoise Culard},
  journal={Biochemistry},
  year={1996},
  volume={35 24},
  pages={7954-8}
}
The interaction of the archaebacterial MC1 protein with 207 bp negatively supercoiled DNA minicircles has been examined by gel retardation assays and compared to that observed with the relaxed DNA minicircle. MC1 binding induces a drastic DNA conformational change of each minicircle, leading to an increase of the electrophoretic mobility of the DNA. A slight increase in salt concentration enhances the amount of bound MC1, and high NaCl concentrations are required to dissociate the complexes… CONTINUE READING