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Originally published In Press as doi:10.1074/jbc.M500264200 on May 16, 2005

J. Biol. Chem., Vol. 280, Issue 30, 28072-28084, July 29, 2005
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Biochemical Analysis of the DNA Unwinding and Strand Annealing Activities Catalyzed by Human RECQ1*

Sudha Sharma{ddagger}, Joshua A. Sommers{ddagger}, Saba Choudhary{ddagger}, Jinnifer Korin Faulkner{ddagger}, Sheng Cui§, Lucia Andreoli§, Laura Muzzolini§, Alessandro Vindigni§, and Robert M. Brosh, Jr.{ddagger}

From the {ddagger}Laboratory of Molecular Gerontology, NIA, National Institutes of Health, Baltimore, Maryland 21224 and the §International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Italy

RecQ helicases play an important role in preserving genomic integrity, and their cellular roles in DNA repair, recombination, and replication have been of considerable interest. Of the five human RecQ helicases identified, three are associated with genetic disorders characterized by an elevated incidence of cancer or premature aging: Werner syndrome, Bloom syndrome, and Rothmund-Thomson syndrome. Although the biochemical properties and protein interactions of the WRN and BLM helicases defective in Werner syndrome and Bloom syndrome, respectively, have been extensively investigated, less information is available concerning the functions of the other human RecQ helicases. We have focused our attention on human RECQ1, a DNA helicase whose cellular functions remain largely uncharacterized. In this work, we have characterized the DNA substrate specificity and optimal cofactor requirements for efficient RECQ1-catalyzed DNA unwinding and determined that RECQ1 has certain properties that are distinct from those of other RecQ helicases. RECQ1 stably bound to a variety of DNA structures, enabling it to unwind a diverse set of DNA substrates. In addition to its DNA binding and helicase activities, RECQ1 catalyzed efficient strand annealing between complementary single-stranded DNA molecules. The ability of RECQ1 to promote strand annealing was modulated by ATP binding, which induced a conformational change in the protein. The enzymatic properties of the RECQ1 helicase and strand annealing activities are discussed in the context of proposed cellular DNA metabolic pathways that are important in the maintenance of genomic stability.

Received for publication, January 7, 2005 , and in revised form, May 16, 2005.

* The work was supported in part by a grant from the Human Frontier Science Program, by an Fondogli Investmenti della Ricerca di Base (FIRB) grant from the Ministero dell'Istruzione dell'Università e della Ricerca, and by Grant 02.00648.ST97 from the Consiglio Nazionale delle Ricerche (Rome). 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 Figs. 1-3.

To whom correspondence should be addressed: Laboratory of Molecular Gerontology, NIA, NIH, 5600 Nathan Shock Dr., Baltimore, MD 21224. Tel.: 410-558-8578; Fax: 410-558-8157; E-mail: BroshR{at}grc.nia.nih.gov.


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