Arm sequences contribute to the architecture and catalytic function of a lambda integrase-Holliday junction complex

Radman-Livaja, M.; Shaw, C.; Azaro, M.; Biswas, T.; Ellenberger, T.; Landy, A.

Mol Cell

2003-03 / vol 11 / pages 783-94


lambda integrase (Int) mediates recombination between attachment sites on lambda phage and E. coli DNAs. With the assistance of accessory proteins that induce DNA loops, Int bridges pairs of distinct arm- and core-type DNA binding sites to form synapsed recombination complexes, which then recombine via a Holliday junction (HJ) intermediate. We show that, in addition to promoting the proper positioning of Int protomers, the arm sequences facilitate the catalytic activities of the Int tetramer, independent of accessory proteins or physical continuity between the arm and core sites. We have determined the architecture of ternary complexes containing a HJ, Int, and P’1,2 arm-type DNA. These structures accommodate simultaneous binding of Int to direct-repeat arm sites and indirect-repeat core sites and afford a new view of the higher-order recombinogenic complexes.

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1097-2765 (Print) 1097-2765 (Linking)

IGMM team(s) involved in this publication

Time Factors; Nucleic Acid Conformation; *Recombination, Genetic; Fluorescence Resonance Energy Transfer; Bacteriophage lambda/*enzymology; Catalysis; Catalytic Domain; DNA/*chemistry/genetics/metabolism; Dose-Response Relationship, Drug; Escherichia coli/*metabolism; Microscopy, Fluorescence; Oligonucleotides/chemistry

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