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TitleReplication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2725, Year 2023
Publish dateMay 11, 2023
AuthorsAlexander T Duckworth / Peter L Ducos / Sarah D McMillan / Kenneth A Satyshur / Katelien H Blumenthal / Haley R Deorio / Joseph A Larson / Steven J Sandler / Timothy Grant / James L Keck /
PubMed AbstractBacterial replisomes often dissociate from replication forks before chromosomal replication is complete. To avoid the lethal consequences of such situations, bacteria have evolved replication restart ...Bacterial replisomes often dissociate from replication forks before chromosomal replication is complete. To avoid the lethal consequences of such situations, bacteria have evolved replication restart pathways that reload replisomes onto prematurely terminated replication forks. To understand how the primary replication restart pathway in E. coli (PriA-PriB) selectively acts on replication forks, we determined the cryogenic-electron microscopy structure of a PriA/PriB/replication fork complex. Replication fork specificity arises from extensive PriA interactions with each arm of the branched DNA. These interactions reshape the PriA protein to create a pore encircling single-stranded lagging-strand DNA while also exposing a surface of PriA onto which PriB docks. Together with supporting biochemical and genetic studies, the structure reveals a switch-like mechanism for replication restart initiation in which restructuring of PriA directly couples replication fork recognition to PriA/PriB complex formation to ensure robust and high-fidelity replication re-initiation.
External linksNat Commun / PubMed:37169801 / PubMed Central
MethodsEM (single particle)
Resolution3.22 Å
Structure data

28959

8fak

EMDB-28959, PDB-8fak:
DNA replication fork binding triggers structural changes in the PriA DNA helicase that regulate the PriA-PriB replication restart pathway in E. coli
Method: EM (single particle) / Resolution: 3.22 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • Escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
  • synthetic construct (others)
KeywordsHELICASE/DNA / PriA / PriB / replication restart / E. coli / HELICASE-DNA complex

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