Role of interaction between two silkworm RecA homologs in homologous DNA pairing.
Recombinant BmRad51 and BmDmc1, silkworm homologs of the Escherichia coli RecA proteins catalyzing the homologous DNA pairing, were purified from E. coli cells carrying expression vectors. These possessed different enzymatic properties in the joint molecule formation between single-stranded circular DNA and homologous linear double-stranded DNA. The requirement of single-stranded circular DNA for the efficient reaction was twofold higher in BmRad51 than in BmDmc1. Although able to mediate the joint molecule formation independently, a complex of the two enzymes formed prior to single-stranded DNA binding was found to have augmented efficiency of the pairing reaction.
Kusakabe
T
T
Laboratory of Silkworm Sciences, Kyusyu University Graduate School of Bioresource and Bioenvironmental Sciences, Fukuoka, Japan. kusakabe@agr.kyushu-u.ac.jp
Kawaguchi
Y
Y
Maeda
T
T
Koga
K
K
D000818:Animals; D012831:Bombyx; D018797:Cell Cycle Proteins; D004247:DNA / Q000378:metabolism*; D004270:DNA, Circular; D018076:DNA, Complementary / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000378:metabolism; D005822:Genetic Vectors; D015636:Magnesium Chloride / Q000494:pharmacology; D011485:Protein Binding; D051135:Rad51 Recombinase; D011938:Rec A Recombinases / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
D018797:Cell Cycle Proteins; D004270:DNA, Circular; D018076:DNA, Complementary; D004277:DNA, Single-Stranded; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D015636:Magnesium Chloride; D004247:DNA; D051135:Rad51 Recombinase; D011938:Rec A Recombinases