ParB is an unusual DNA binding protein. In addition to sequence-specific interactions with the parS sequence, the protein also spreads extensively around the site for about 18 kbp. However, the mechanistic basis for this behaviour is not well understood and a matter of active debate. We have used our single-molecule tools to investigate the binding of B.subtilis ParB to DNA in vitro.
Topic-related papers of the group
Gemma LM Fisher*, Cesar L Pastrana*, Victoria A Higman* et al. Elife Dec 15;6 (2017) pii: e28086. doi: 10.7554/eLife.28086. The structural basis for dynamic DNA binding and bridging interactions which condense the bacterial centromere. LINK
Taylor*, Pastrana* et al. Nucleic Acids Research 43(2), 719-731 (2015). Specific and non-specific interactions of ParB with DNA: implications for chromosome segregation. LINK
Collaborators
University of Bristol: Mark Dillingham Group