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• W1970258574 startingPage "1457" @default.
• W1970258574 abstract "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." @default.
• W1970258574 created "2016-06-24" @default.
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• W1970258574 date "1989-06-23" @default.
• W1970258574 modified "2023-09-28" @default.
• W1970258574 title "DNA Looping Generated by DNA Bending Protein IHF and the Two Domains of Lambda Integrase" @default.
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• W1970258574 doi "https://doi.org/10.1126/science.2544029" @default.
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