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Papers In Press, published online ahead of print December 20, 2000
Molecular Medicine and Institute of Biotechnology, University of Texas San Antonio, San Antonio, TX 78245
Corresponding Author: sung{at}uthscsa.edu
Human Rad51 (hRad51), 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 kilo base pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric ssDNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-ssDNA 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.
J. Biol. Chem, 10.1074/jbc.M010011200
Submitted on November 3, 2000
Revised on December 12, 2000
Accepted on December 19, 2000
Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA
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