DNA arms do the legwork to ensure the directionality of lambda site-specific recombination.
The integrase protein of bacteriophage lambda (Int) catalyzes site-specific recombination between lambda phage and Escherichia coli genomes. Int is a tyrosine recombinase that binds to DNA core sites via a C-terminal catalytic domain and to a collection of arm DNA sites, distant from the site of recombination, via its N-terminal domain. The arm sites, in conjunction with accessory DNA-bending proteins, provide a means of regulating the efficiency and directionality of Int-catalyzed recombination. Recent crystal structures of lambda Int tetramers bound to synaptic and Holliday junction intermediates, together with new biochemical data, suggest a mechanism for the allosteric control of the recombination reaction through arm DNA binding interactions.
Radman-Livaja
Marta
M
Division of Biology and Medicine-Box G, Brown University, Providence, RI 02912, USA.
Biswas
Tapan
T
Ellenberger
Tom
T
Landy
Arthur
A
Aihara
Hideki
H
D010582:Bacteriophage lambda / Q000201:enzymology / Q000235:genetics*; D004279:DNA, Viral / Q000502:physiology*; D019426:Integrases / Q000235:genetics / Q000502:physiology*; D011995:Recombination, Genetic; D016662:Virus Integration / Q000502:physiology*
D004279:DNA, Viral; D019426:Integrases