Abstract
Recombination reactions were performed between ColE1 DNA bound to cellulose (DNA-cellulose) and 3H-labeled ColE1 DNA in a crude extract prepared from T7-infected cells. The amount of binding of radioactivity to DNA-cellulose depended on the presence of T7 exonuclease, which is indispensable for T7 genetic recombination in vivo. The binding reaction was specific for homologous DNA. Applying this assay to the purification of enzymes which are essential for T7 genetic recombination, a protein factor was found in the extracts from T7-infected cells, which works in cooperation with T7 exonuclease. The protein was tentatively identified as the T7 DNA-binding protein, on the basis of purification and its molecular weight (32,000). This identification was supported by the isolation of a T7 mutant defective in DNA-binding protein; which displays a 10-fold lower frequency of recombination than wild-type T7.
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