Radman-Livaja Marta, Biswas Tapan, Ellenberger Tom, Landy Arthur, Aihara Hideki
Division of Biology and Medicine-Box G, Brown University, Providence, RI 02912, USA.
Curr Opin Struct Biol. 2006 Feb;16(1):42-50. doi: 10.1016/j.sbi.2005.12.003. Epub 2005 Dec 20.
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.
噬菌体λ的整合酶蛋白(Int)催化λ噬菌体与大肠杆菌基因组之间的位点特异性重组。Int是一种酪氨酸重组酶,它通过C端催化结构域与DNA核心位点结合,并通过其N端结构域与远离重组位点的一系列臂DNA位点结合。臂位点与辅助DNA弯曲蛋白一起,提供了一种调节Int催化重组效率和方向性的方式。最近与突触和霍利迪连接中间体结合的λ Int四聚体的晶体结构,以及新的生化数据,提示了一种通过臂DNA结合相互作用对重组反应进行变构控制的机制。