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Science 23 June 1989:
Vol. 244. no. 4911, pp. 1457 - 1461
DOI: 10.1126/science.2544029
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Articles

Science, Vol 244, Issue 4911, 1457-1461
Copyright © 1989 by American Association for the Advancement of Science

articles

DNA looping generated by DNA bending protein IHF and the two domains of lambda integrase

L Moitoso de Vargas, S Kim, and A Landy

Division of Biology and Medicine, Brown University, Providence, RI 02912.

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.


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