Holliday intermediates and reaction by-products in FLP protein-promoted site-specific recombination.
Holliday structures are formed and resolved by FLP protein during site-specific recombination. These structures have been isolated and are visualized in both native and partially denatured states by electron microscopy. No single-strand breaks are found within the junction, indicating that the structure results from a reciprocal exchange of strands. These structures have properties consistent with being reaction intermediates. Double-strand cleavage products and "Y structures" are also detected and appear to be by-products of the reaction. The Y structures are three-armed branched molecules with a covalently closed junction located at the FLP recombination target site. Models are discussed, suggesting that both of these novel structures are made by aberrant cleavages during formation and resolution of the Holliday intermediate.
Meyer-Leon
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L
Department of Biochemistry, College of Agriculture and Life Sciences, University of Wisconsin-Madison 53706-1569.
Huang
L C
LC
Umlauf
S W
SW
Cox
M M
MM
Inman
R B
RB
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D004247:DNA / Q000235:genetics / Q000648:ultrastructure*; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D008854:Microscopy, Electron; D009154:Mutation; D010957:Plasmids; D011995:Recombination, Genetic; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D013379:Substrate Specificity
D001425:Bacterial Outer Membrane Proteins; D004247:DNA; D004254:DNA Nucleotidyltransferases; C045119:FLP recombinase