Asymmetry in active complexes of FLP recombinase.
The FLP recombinase promotes a site-specific recombination reaction in the 2mu plasmid of yeast. The protein-DNA complex that carries out the reaction is asymmetric. Three FLP monomers bound to specific FLP-recognition sequences are required to efficiently carry out one set of reciprocal DNA cleavage and strand exchange events on a Holliday junction substrate. If a fourth monomer plays an auxiliary role in the reaction, it is bound without sequence specificity. The data suggest a modified model for cleavage of DNA in trans by the FLP recombinase that might help reconcile some seemingly conflicting resulted obtained with integrase class recombinases.
Qian
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XH
Department of Biochemistry, University of Wisconsin-Madison 53706, USA.
Cox
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D001483:Base Sequence; D001665:Binding Sites; D004254:DNA Nucleotidyltransferases / Q000737:chemistry / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D011995:Recombination, Genetic; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism*; D013379:Substrate Specificity
D005656:Fungal Proteins; D046911:Macromolecular Substances; D011994:Recombinant Proteins; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase