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.
journal_name
Proc Natl Acad Sci U S Aauthors
Pike AC,Gomathinayagam S,Swuec P,Berti M,Zhang Y,Schnecke C,Marino F,von Delft F,Renault L,Costa A,Gileadi O,Vindigni Adoi
10.1073/pnas.1417594112subject
Has Abstractpub_date
2015-04-07 00:00:00pages
4286-91issue
14eissn
0027-8424issn
1091-6490pii
1417594112journal_volume
112pub_type
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