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- Title
Examination of the roles of a conserved motif in the PriA helicase in structure-specific DNA unwinding and processivity.
- Authors
Duckworth, Alexander T.; Windgassen, Tricia A.; Keck, James L.
- 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 potential autoregulatory element in replication fork processing. The study also suggests that multiple PriA molecules may function in tandem to enhance DNA unwinding processivity, highlighting an unexpected similarity between PriA and other DNA helicases.
- Subjects
DNA helicases; DNA denaturation; DNA replication; REPLISOMES; ESCHERICHIA coli; MOLECULES
- Publication
PLoS ONE, 2021, Vol 16, Issue 7, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0255409