The mechanism of loading of the FLP recombinase onto its DNA target sequence.
The FLP recombinase interacts with its target sequence with the formation of three distinct DNA-protein complexes. The first complex leaves neither a DNase footprint nor is the DNA protected from methylation by dimethyl sulfate. We have found, however, that the FLP protein is bound predominantly to only one of the three 13 base-pair (bp) symmetry elements. This asymmetric loading of the FLP site seems to require the presence of an adjacent directly repeated 13 bp element. We speculate that this asymmetric filling of the target site may be accompanied by the unique order of cleavage and exchange of DNA strands.
Beatty
L G
LG
Department of Medical Genetics, University of Toronto, Ontario, Canada.
Sadowski
P D
PD
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004269:DNA, Bacterial / Q000378:metabolism*; D004926:Escherichia coli; D005092:Exonucleases / Q000378:metabolism; D046911:Macromolecular Substances; D008745:Methylation; D008969:Molecular Sequence Data; D010710:Phosphates / Q000378:metabolism; D010957:Plasmids; D011995:Recombination, Genetic
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D004269:DNA, Bacterial; D046911:Macromolecular Substances; D010710:Phosphates; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase; D005092:Exonucleases