The FLP recombinase of the Saccharomyces cerevisiae 2 microns plasmid attaches covalently to DNA via a phosphotyrosyl linkage.
The FLP recombinase, encoded by the 2 micron plasmid of Saccharomyces cerevisiae, promotes efficient recombination in vivo and in vitro between its specific target sites (FLP sites). It was previously determined that FLP interacts with DNA sequences within its target site (B. J. Andrews, G. A. Proteau, L. G. Beatty, and P. D. Sadowski. Cell 40:795-803, 1985), generates a single-stranded break on both DNA strands within the FLP site, and remains covalently attached to the 3' end of each break. We now show that the FLP protein is bound to the 3' side of each break by an O-phosphotyrosyl residue and that it appears that the same tyrosyl residue(s) is used to attach to either DNA strand within the FLP site.
D001483:Base Sequence; D002872:Chromosome Deletion; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D004271:DNA, Fungal / Q000378:metabolism*; D006868:Hydrolysis; D019000:Phosphotyrosine; D010957:Plasmids; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D014443:Tyrosine / Q000031:analogs & derivatives*
D004271:DNA, Fungal; D019000:Phosphotyrosine; D014443:Tyrosine; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase; D004262:DNA Restriction Enzymes