DNA arms do the legwork to ensure the directionality of lambda site-specific recombination

Radman-Livaja, M.; Biswas, T.; Ellenberger, T.; Landy, A.; Aihara, H.

Current opinion in structural biology

2006-02 / vol 16 / pages 42-50


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.

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0959-440X (Print) 0959-440X (Linking)

IGMM team(s) involved in this publication

*Recombination, Genetic; Bacteriophage lambda/enzymology/*genetics; DNA, Viral/*physiology; Integrases/genetics/*physiology; Virus Integration/*physiology

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