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

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-te

SUBMITTER: Pike AC 

PROVIDER: S-EPMC4394259 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature