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Unraveling RecQ helicase dynamics one molecule at a time

Tuesday, October 09, 2012 — Poster Session I

1:00 p.m. – 3:00 p.m

Natcher Conference Center, Building 45




  • RM Harrison
  • SK Sarkar
  • AN Kapanidis
  • KC Neuman


Helicases are ATP-dependent translocates essential to genome integrity through their role in replication, recombination and repair. As such, they are highly conserved in prokaryotes and eukaryotes, from E. coli to man. In humans, heritable defects in helicases such as Wrn and Blm manifest clinically as premature aging and a greatly elevated cancer risk. These clinical manifestations follow from aberrant recombination and deficient damage repair. Despite their important biological role, the mechanisms by which helicases translocate on and unwind their substrates remains poorly understood. Although several models have been proposed to describe the mechanics of SF 1/2 helicases based on biochemical and structural data, none have been verified at the single-molecule level. We wish to elucidate the mechanism of RecQ, a prototypical DNA helicase representative of SF2 helicases. Specifically, we will use single-molecule fluorescence to directly probe the oligomerization state and inter-domain motions of RecQ.

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