RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination.

Abstract

E. coli RecQ protein is a multifunctional helicase with homologs that include the S. cerevisiae Sgs1 helicase and the H. sapiens Wrn and Blm helicases. Here we show that RecQ helicase unwinds a covalently closed double-stranded DNA (dsDNA) substrate and that this activity specifically stimulates E. coli topoisomerase III (Topo III) to fully catenate dsDNA molecules. We propose that these proteins functionally interact and that their shared activity is responsible for control of DNA recombination. RecQ helicase has a comparable effect on the Topo III homolog of S. cerevisiae, consistent with other RecQ and Topo III homologs acting together in a similar capacity. These findings highlight a novel, conserved activity that offers insight into the function of the other RecQ-like helicases.

Extracted Key Phrases

6 Figures and Tables

Statistics

02040'01'03'05'07'09'11'13'15'17
Citations per Year

277 Citations

Semantic Scholar estimates that this publication has 277 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Harmon1999RecQHA, title={RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination.}, author={Frank G Harmon and Russell J Digate and Stephen C Kowalczykowski}, journal={Molecular cell}, year={1999}, volume={3 5}, pages={611-20} }