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I04-Macromolecular Crystallography	Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: Insights from DNA complex structures Ashley Pike , Shivasankari Gomathinayagam , Paolo Swuec , Matteo Berti , Ying Zhang , Christina Schnecke , Francesca Marino , Frank Von Delft , Ludovic Renault , Alessandro Costa , Opher Gileadi , Alessandro Vindigni Proceedings Of The National Academy Of Sciences 112 (14), 4286 - 4291 DOI: 10.1073/pnas.1417594112 PMID: 25831490 Diamond Proposal Number(s): [442] Open Access Show Abstract ▼ Abstract: RecQ helicases are a widely conserved family of ATP-dependent motors with diverse roles in nearly every aspect of bacterial and eukaryotic genome maintenance. However, the physical mechanisms by which RecQ helicases recognize and process specific DNA replication and repair intermediates are largely unknown. Here, we solved crystal structures of the human RECQ1 helicase in complexes with tailed-duplex DNA and ssDNA. The structures map the interactions of the ssDNA tail and the branch point along the helicase and Zn-binding domains, which, together with reported structures of other helicases, define the catalytic stages of helicase action. We also identify a strand-separating pin, which (uniquely in RECQ1) is buttressed by the protein dimer interface. A duplex DNA-binding surface on the C-terminal domain is shown to play a role in DNA unwinding, strand annealing, and Holliday junction (HJ) branch migration. We have combined EM and analytical ultracentrifugation approaches to show that RECQ1 can form what appears to be a flat, homotetrameric complex and propose that RECQ1 tetramers are involved in HJ recognition. This tetrameric arrangement suggests a platform for coordinated activity at the advancing and receding duplexes of an HJ during branch migration.	Apr 2015

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I04-Macromolecular Crystallography

Human RECQ1 helicase-driven DNA unwinding, annealing, and branch migration: Insights from DNA complex structures