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J. Biol. Chem., Vol. 283, Issue 29, 20231-20242, July 18, 2008

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RECQ1 Possesses DNA Branch Migration Activity^*

Dmitry V. Bugreev, Robert M. Brosh, Jr.^¶, and Alexander V. Mazin¹

From the Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102-1192, the Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Science, Novosibirsk 630090, Russia, and the ^¶Laboratory of Molecular Gerontology, NIA, National Institutes of Health, Baltimore, Maryland 21224

RecQ helicases are essential for the maintenance of genome stability. Five members of the RecQ family have been found in humans, including RECQ1, RECQ5, BLM, WRN, and RECQ4; the last three are associated with human diseases. At this time, only BLM and WRN helicases have been extensively characterized, and the information on the other RecQ helicases has only started to emerge. Our current paper is focused on the biochemical properties of human RECQ1 helicase. Recent cellular studies have shown that RECQ1 may participate in DNA repair and homologous recombination, but the exact mechanisms of how RECQ1 performs its cellular functions remain largely unknown. Whereas RECQ1 possesses poor helicase activity, we found here that the enzyme efficiently promotes DNA branch migration. Further analysis revealed that RECQ1 catalyzes unidirectional three-stranded branch migration with a 3' 5' polarity. We show that this RECQ1 activity is instrumental in specific disruption of joint molecules (D-loops) formed by a 5' single-stranded DNA invading strand, which may represent dead end intermediates of homologous recombination in vivo. The newly found enzymatic properties of the RECQ1 helicase may have important implications for the function of RECQ1 in maintenance of genomic stability.

Received for publication, February 27, 2008 , and in revised form, May 1, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grant CA100839 and by a grant from the Intramural Research Program of NIA, National Institutes of Health (to R. M. B., Jr.). This work was also supported by Leukemia and Lymphoma Society Scholar Award 1054-09 (to A. V. M.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S1 and supplemental Figs. S1–S5.

¹ To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Drexel University College of Medicine, 245 N 15th St., NCB, Rm. 10103, Philadelphia, PA 19102-1192. Tel.: 215-762-7195; Fax: 215-762-4452; E-mail: amazin{at}drexelmed.edu.

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