Dynamics of the E. coli β-Clamp Dimer Interface and Its Influence on DNA Loading.

ABSTRACT: The ring-shaped sliding clamp proteins have crucial roles in the regulation of DNA replication, recombination, and repair in all organisms. We previously showed that the Escherichia coli β-clamp is dynamic in solution, transiently visiting conformational states in which Domain 1 at the dimer interface is more flexible and prone to unfolding. This work aims to understand how the stability of the dimer interface influences clamp-opening dynamics and clamp loading by designing and characterizing stabilizing and destabilizing mutations in the clamp. The variants with stabilizing mutations conferred similar or increased thermostability and had similar quaternary structure as compared to the wild type. These variants stimulated the ATPase function of the clamp loader, complemented cell growth of

SUBMITTER: Koleva BN 

PROVIDER: S-EPMC6697468 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature