Structural mechanisms of PriA-mediated DNA replication restart.

ABSTRACT: Collisions between cellular DNA replication machinery (replisomes) and damaged DNA or immovable protein complexes can dissociate replisomes before the completion of replication. This potentially lethal problem is resolved by cellular "replication restart" reactions that recognize the structures of prematurely abandoned replication forks and mediate replisomal reloading. In bacteria, this essential activity is orchestrated by the PriA DNA helicase, which identifies replication forks via structure-specific DNA binding and interactions with fork-associated ssDNA-binding proteins (SSBs). However, the mechanisms by which PriA binds replication fork DNA and coordinates subsequent replication restart reactions have remained unclear due to the dearth of high-resolution structural information avail

SUBMITTER: Bhattacharyya B 

PROVIDER: S-EPMC3910646 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature