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Originally published In Press as doi:10.1074/jbc.M010011200 on December 20, 2000

J. Biol. Chem., Vol. 276, Issue 12, 8798-8806, March 23, 2001
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Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA*

Stefan Sigurdsson, Kelly Trujillo, BinWei Song, Sabrina Stratton, and Patrick SungDagger

From the Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245-3207

Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.

* This work was supported by United States Public Health Service Grants RO1 ES07061, RO1GM57814, and PO1 CA81020, Army Research Grant DAMD 17-98-1-8247, and Army Training Grant DAMD17-99-1-9402.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 210-567-7216; Fax: 210-567-7277; E-mail: sung@uthscsa.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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