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

Lina Moitoso De Vargas, Sunghoon Kim, Arthur Landy

Research output: Contribution to journalArticle

138 Citations (Scopus)

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 coretype 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.

Original languageEnglish
Pages (from-to)1457-1461
Number of pages5
JournalScience
Volume244
Issue number4911
DOIs
Publication statusPublished - 1989

All Science Journal Classification (ASJC) codes

  • General

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