Arm sequences contribute to the architecture and catalytic function of a lambda integrase-Holliday junction complex.
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.
Radman-Livaja
Marta
M
Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Box G-J360, Providence, RI 02912, USA.
Shaw
Christine
C
Azaro
Marco
M
Biswas
Tapan
T
Ellenberger
Tom
T
Landy
Arthur
A
D010582:Bacteriophage lambda / Q000201:enzymology*; D002384:Catalysis; D020134:Catalytic Domain; D004247:DNA / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004926:Escherichia coli / Q000378:metabolism*; D031541:Fluorescence Resonance Energy Transfer; D008856:Microscopy, Fluorescence; D009690:Nucleic Acid Conformation; D009841:Oligonucleotides / Q000737:chemistry; D011995:Recombination, Genetic; D013997:Time Factors
D009841:Oligonucleotides; D004247:DNA