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Originally published In Press as doi:10.1074/jbc.M414130200 on April 20, 2005

J. Biol. Chem., Vol. 280, Issue 24, 23397-23407, June 17, 2005
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RecQ Family Members Combine Strand Pairing and Unwinding Activities to Catalyze Strand Exchange*

Amrita Machwe{ddagger}, Liren Xiao{ddagger}, Joanna Groden§, Steven W. Matson¶, and David K. Orren{ddagger}||

From the {ddagger}Graduate Center for Toxicology, University of Kentucky, Lexington, Kentucky 40536-0305, the §Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267, and the Department of Biology, University of North Carolina, Chapel Hill, North Carolina 27599

RecQ helicases are critical for maintaining genomic integrity. In this study, we show that three RecQ members (WRN, deficient in the Werner syndrome; BLM, deficient in the Bloom syndrome; and Drosophila melanogaster RecQ5b (dmRecQ5b)) possess a novel strand pairing activity. Furthermore, each of these enzymes combines this strand pairing activity with its inherent DNA unwinding capability to perform coordinated strand exchange. In this regard, WRN and BLM are considerably more efficient than dmRecQ5b, apparently because dmRecQ5b lacks conserved sequences C-terminal to the helicase domain that contribute to DNA binding, strand pairing, and strand exchange. Based on our findings, we postulate that certain RecQ helicases are structurally designed to accomplish strand exchange on complex replication and recombination intermediates. This is highly consistent with proposed roles for RecQ members in DNA metabolism and the illegitimate recombination and cancer-prone phenotypes associated with RecQ defects.


Received for publication, December 16, 2004 , and in revised form, April 7, 2005.

* This work was supported by grants from the Ellison Medical Foundation and the University of Kentucky Research Foundation (to D. K. O.) and by NCI Grant R01 CA113371-01 from the National Institutes of Health (to D. K. O.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Graduate Center for Toxicology, 356 Health Sciences Research Bldg., University of Kentucky, 800 Rose St., Lexington, KY 40536-0305. Tel.: 859-323-3612; Fax: 859-323-1059; E-mail: dkorre2{at}uky.edu.


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