Basis for avid homologous DNA strand exchange by human Rad51 and RPA.
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.
Sigurdsson
S
S
Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78245-3207, USA.
Trujillo
K
K
Song
B
B
Stratton
S
S
Sung
P
P
D010584:Bacteriophage phi X 174 / Q000235:genetics; D001483:Base Sequence; D017931:DNA Primers; D004277:DNA, Single-Stranded / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D051135:Rad51 Recombinase; D011995:Recombination, Genetic; D051716:Replication Protein A
D017931:DNA Primers; D004277:DNA, Single-Stranded; D004279:DNA, Viral; D004268:DNA-Binding Proteins; C497167:RPA1 protein, human; D051716:Replication Protein A; C495153:RAD51 protein, human; D051135:Rad51 Recombinase