Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.

ABSTRACT: DNA replication complexes (replisomes) frequently encounter barriers that can eject them prematurely from the genome. To avoid the lethality of incomplete DNA replication that arises from these events, bacteria have evolved "DNA replication restart" mechanisms to reload replisomes onto abandoned replication forks. The Escherichia coli PriA DNA helicase orchestrates this process by recognizing and remodeling replication forks and recruiting additional proteins that help to drive replisome reloading. We have identified a conserved sequence motif within a linker region of PriA that docks into a groove on the exterior of the PriA helicase domain. Alterations to the motif reduce the apparent processivity and attenuate structure-specific helicase activity in PriA, implicating the motif as a pote

SUBMITTER: Duckworth AT 

PROVIDER: S-EPMC8323898 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature