DNA arms do the legwork to ensure the directionality of lambda site-specific recombination |
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Authors: | Radman-Livaja Marta Biswas Tapan Ellenberger Tom Landy Arthur Aihara Hideki |
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Institution: | Division of Biology and Medicine-Box G, Brown University, Providence, RI 02912, USA. |
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Abstract: | 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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