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Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.

Proc. Natl. Acad. Sci. U.S.A.2018 Sep 25;115(39):E9075-E9084. Epub 2018 Sep 10
Tricia A Windgassen 1 , Maxime Leroux 2 , Kenneth A Satyshur 1 , Steven J Sandler 2 , James L Keck 3
Tricia A Windgassen 1 , Maxime Leroux 2 , Kenneth A Satyshur 1 , Steven J Sandler 2 , James L Keck 3

[No authors listed]

Author information
  • 1 Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706.
  • 2 Department of Microbiology, University of Massachusetts Amherst, Amherst, MA 01003.
  • 3 Department of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, WI 53706; jlkeck@wisc.edu.

摘要


DNA replication restart, the essential process that reinitiates prematurely terminated genome replication reactions, relies on exquisitely specific recognition of abandoned DNA replication-fork structures. The PriA DNA helicase mediates this process in bacteria through mechanisms that remain poorly defined. We report the crystal structure of a PriA/replication-fork complex, which resolves leading-strand duplex DNA bound to the protein. Interaction with PriA unpairs one end of the DNA and sequesters the 3'-most nucleotide from the nascent leading strand into a conserved protein pocket. Cross-linking studies reveal a surface on the winged-helix domain of PriA that binds to parental duplex DNA. Deleting the winged-helix domain alters PriA's structure-specific DNA unwinding properties and impairs its activity in vivo. Our observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks.

KEYWORDS: DNA repair, DNA replication restart, X-ray crystallography, cross-link mapping, protein–DNA complex