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J. Biol. Chem., Vol. 267, Issue 24, 16755-16758, Aug, 1992
S Shuman
The ability of a eukaryotic DNA topoisomerase I to catalyze DNA
rearrangements was examined in vitro using defined substrates and purified
enzyme. Site-specific DNA strand cleavage by vaccinia topoisomerase I
across from a nick generated double-strand breaks that could be religated
to a heterologous blunt-ended duplex DNA regardless of the sequence of the
acceptor molecule. Topoisomerase bound covalently at internal positions
could religate the bound strand to an incoming acceptor provided that DNA
molecule had sequence homology to the region 3' of the scissile bond. These
end-joining reactions suggest two potential modes of topoisomerase-mediated
recombination that differ in their requirements for DNA homology.
Two classes of DNA end-joining reactions catalyzed by vaccinia topoisomerase I
Program in Molecular Biology, Sloan-Kettering Institute, New York, New York 10021.
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