Ligation activity of FLP recombinase. The strand ligation activity of a site-specific recombinase using an activated DNA substrate.
The FLP protein of the 2-microns plasmid of yeast belongs to the integrase family of site-specific recombinases whose members form a covalent bond between a conserved tyrosine of the recombinase and the 3'-phosphoryl group at the site of cleavage. We have made an activated DNA substrate and have shown that FLP can promote efficient strand ligation without forming a covalent intermediate with the DNA substrate. The strand ligation activity of FLP is independent of its ability to cleave DNA. Since site-specific recombinases are members of the larger class of topoisomerases, these findings may be generally applicable to other members of this class of enzymes.
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Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.
Sadowski
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D001483:Base Sequence; D004247:DNA / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D003854:Deoxyribonucleotides / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013379:Substrate Specificity
D003854:Deoxyribonucleotides; D005656:Fungal Proteins; D004247:DNA; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase