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J. Biol. Chem., Vol. 275, Issue 21, 15895-15904, May 26, 2000
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From the Department of Molecular Medicine/Institute of
Biotechnology, University of Texas Health Science Center,
San Antonio, Texas 78245-3207
Rad51-catalyzed DNA strand exchange is greatly
enhanced by the single-stranded (ss) DNA binding factor RPA if the
latter is introduced after Rad51 has already nucleated onto the
initiating ssDNA substrate. Paradoxically, co-addition of RPA with
Rad51 to the ssDNA to mimic the in vivo situation
diminishes the level of strand exchange, revealing competition between
RPA and Rad51 for binding sites on ssDNA. Rad52 promotes strand
exchange but only when there is a need for Rad51 to compete with RPA
for loading onto ssDNA. Rad52 is multimeric, binds ssDNA, and targets
Rad51 to ssDNA. Maximal restoration of pairing and strand exchange
requires amounts of Rad52 substoichiometric to Rad51 and involves a
stable, equimolar complex between Rad51 and Rad52. The Rad51-Rad52
complex efficiently utilizes a ssDNA template saturated with RPA for
homologous pairing but does not appear to be more active than Rad51
when an RPA-free ssDNA template is used. Rad52 does not substitute for
RPA in the pairing and strand exchange reaction nor does it lower the
dependence of the reaction on Rad51 or RPA.
Functional Interactions among Yeast Rad51 Recombinase, Rad52
Mediator, and Replication Protein A in DNA Strand Exchange*
*
This work was supported by United States Public Health
Service Grant ES07061 from the NIEHS and by NIGMS Grant GM57814 from the National Institutes of Health.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.
To whom correspondence should be addressed: Dept. of Molecular
Medicine/Inst. of Biotechnology, University of Texas Health Science
Center, 15355 Lambda Dr., San Antonio, TX 78245-3207. Tel.:
210-567-7216; Fax: 210-567-7277; E-mail: sung@uthscsa.edu.
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