CTP promotes efficient ParB-dependent DNA condensation by facilitating one-dimensional diffusion from <i>par</i>S.

ABSTRACT: Faithful segregation of bacterial chromosomes relies on the ParABS partitioning system and the SMC complex. In this work, we used single-molecule techniques to investigate the role of cytidine triphosphate (CTP) binding and hydrolysis in the critical interaction between centromere-like parS DNA sequences and the ParB CTPase. Using a combined optical tweezers confocal microscope, we observe the specific interaction of ParB with parS directly. Binding around parS is enhanced by the presence of CTP or the non-hydrolysable analogue CTPγS. However, ParB proteins are also detected at a lower density in distal non-specific DNA. This requires the presence of a parS loading site and is prevented by protein roadblocks, consistent with one-dimensional diffusion by a slidin

SUBMITTER: Balaguer FA 

PROVIDER: S-EPMC8299390 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature