DNA looping generated by DNA bending protein IHF and the two domains of lambda integrase.
The multiprotein-DNA complexes that participate in bacteriophage lambda site-specific recombination were used to study the combined effect of protein-induced bending and protein-mediated looping of DNA. The protein integrase (Int) is a monomer with two autonomous DNA binding domains of different sequence specificity. Stimulation of Int binding and cleavage at the low affinity core-type DNA sites required interactions with the high affinity arm-type sites and depended on simultaneous binding of the sequence-specific DNA bending protein IHF (integration host factor). The bivalent DNA binding protein is positioned at high affinity sites and directed, by a DNA bending protein, to interactions with distant lower affinity sites. Assembly of this complex is independent of protein-protein interactions.
Moitoso de Vargas
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Division of Biology and Medicine, Brown University, Providence, RI 02912.
Kim
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Landy
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D001426:Bacterial Proteins / Q000378:metabolism / Q000494:pharmacology*; D010582:Bacteriophage lambda / Q000201:enzymology / Q000235:genetics*; D001665:Binding Sites; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D004251:DNA Transposable Elements; D004269:DNA, Bacterial / Q000235:genetics / Q000378:metabolism*; D004279:DNA, Viral / Q000235:genetics / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism; D019426:Integrases; D034982:Integration Host Factors; D009154:Mutation; D009690:Nucleic Acid Conformation / Q000187:drug effects*; D011995:Recombination, Genetic
D001426:Bacterial Proteins; D004251:DNA Transposable Elements; D004269:DNA, Bacterial; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D034982:Integration Host Factors; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D004262:DNA Restriction Enzymes