Holliday junctions in FLP recombination: resolution by step-arrest mutants of FLP protein.
The FLP "recombinase" of the 2-micron circle yeast plasmid can resolve synthetic FLP site-Holliday junctions. Mutants of the FLP protein that are blocked in recombination but are normal in substrate cleavage can also mediate resolution. The products of resolution by these mutants are almost exclusively nicked molecules with a protein-bound 3' end. There is no significant asymmetry in strand cleavage (top versus bottom) by the mutants in linear or in circular FLP substrates; nor is there a bias in resolution (toward parentals or toward recombinants) of Holliday junctions (corresponding to top- or to bottom-strand exchange) by wild-type FLP. During normal FLP recombination, a small amount of the expected Holliday intermediate can be detected.
Jayaram
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M
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
Crain
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KL
Parsons
R L
RL
Harshey
R M
RM
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics*; D001483:Base Sequence; D004254:DNA Nucleotidyltransferases / Q000235:genetics*; D004261:DNA Replication; D004269:DNA, Bacterial / Q000032:analysis / Q000648:ultrastructure; D004926:Escherichia coli / Q000235:genetics; D006639:Histidine; D008854:Microscopy, Electron; D009154:Mutation; D009710:Nucleotide Mapping; D011995:Recombination, Genetic
D001425:Bacterial Outer Membrane Proteins; D004269:DNA, Bacterial; D006639:Histidine; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase