Primase is required for helicase activity and helicase alters the specificity of primase in the enteropathogen Clostridium difficile.

ABSTRACT: DNA replication is an essential and conserved process in all domains of life and may serve as a target for the development of new antimicrobials. However, such developments are hindered by subtle mechanistic differences and limited understanding of DNA replication in pathogenic microorganisms. Clostridium difficile is the main cause of healthcare-associated diarrhoea and its DNA replication machinery is virtually uncharacterized. We identify and characterize the mechanistic details of the putative replicative helicase (CD3657), helicase-loader ATPase (CD3654) and primase (CD1454) of C. difficile, and reconstitute helicase and primase activities in vitro We demonstrate a direct and ATP-dependent interaction between the helicase loader and the helicase. Furthermore, we find that helicase act

SUBMITTER: van Eijk E 

PROVIDER: S-EPMC5204125 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature