Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1979622 | Current Opinion in Structural Biology | 2006 | 9 Pages |
Abstract
The integrase protein of bacteriophage λ (Int) catalyzes site-specific recombination between λ 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 λ 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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Authors
Marta Radman-Livaja, Tapan Biswas, Tom Ellenberger, Arthur Landy, Hideki Aihara,