Structure of the human RECQ1 helicase reveals a putative strand-separation pin

Ashley C.W. Pike, Binesh Shrestha, Venkateswarlu Popuri, Nicola Burgess-Brown, Laura Muzzolini, Silvia Costantini, Alessandro Vindigni, Opher Gileadi

Research output: Contribution to journalArticlepeer-review

107 Scopus citations


RecQ-like helicases, which include 5 members in the human genome, are important in maintaining genome integrity. We present a crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP. The truncated protein is active in DNA fork unwinding but lacks other activities of the full-length enzyme: disruption of Holliday junctions and DNA strand annealing. The structure of human RECQ1 resembles that of Escherichia coli RecQ, with some important differences. All structural domains are conserved, including the 2 RecA-like domains and the RecQ-specific zinc-binding and winged-helix (WH) domains. However, the WH domain is positioned at a different orientation from that of the E. coli enzyme. We identify a prominent β-hairpin of the WH domain as essential for DNA strand separation, which may be analogous to DNA strand-separation features of other DNA helicases. This hairpin is significantly shorter in the E. coli enzyme and is not required for its helicase activity, suggesting that there are significant differences between the modes of action of RecQ family members.

Original languageEnglish
Pages (from-to)1039-1044
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number4
StatePublished - Jan 27 2009


  • DNA helicase
  • DNA repair
  • Holliday junction
  • Structural genomics
  • Winged helix


Dive into the research topics of 'Structure of the human RECQ1 helicase reveals a putative strand-separation pin'. Together they form a unique fingerprint.

Cite this