TY - JOUR
T1 - DNA arms do the legwork to ensure the directionality of λ site-specific recombination
AU - Radman-Livaja, Marta
AU - Biswas, Tapan
AU - Ellenberger, Tom
AU - Landy, Arthur
AU - Aihara, Hideki
PY - 2006/2
Y1 - 2006/2
N2 - 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.
AB - 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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U2 - 10.1016/j.sbi.2005.12.003
DO - 10.1016/j.sbi.2005.12.003
M3 - Review article
C2 - 16368232
AN - SCOPUS:32344451042
SN - 0959-440X
VL - 16
SP - 42
EP - 50
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 1
ER -