Protein-protein interactions in a higher-order structure direct lambda site-specific recombination.
Protein-protein interactions in a higher-order structure direct lambda site-specific recombination.
复制标题
高阶结构中的蛋白质-蛋白质相互作用直接 lambda 位点特异性重组。
DOI：
10.1016/0022-2836(87)90177-x
复制
发表时间：
1987
影响因子：
5.6
通讯作者：
Landy,A
中科院分区：
文献类型：
--
作者：
Thompson,JF;deVargas,LM;Skinner,SE;Landy,A
λ噬菌体的高度定向的位点特异性重组受到三种不同蛋白质与一系列复杂位点的结合的严格调控。这些反应的刺激和抑制的方式合作的蛋白质的P臂上的特定位点的attP和dattR的结合已经阐明了相关的核酸酶保护与重组研究的野生型和突变体DNA。除了合作力量，还有一种特殊的竞争相互作用，使蛋白质-DNA复合物成为“生物开关”。这种转换并不依赖于相邻蛋白质对DNA结合位点的简单封闭;相反，这种竞争的结果取决于attP和dattR的高阶结构之间的长程相互作用。这些高阶结构依赖于涉及三种蛋白质结合到五个或更多位点的合作相互作用。
The highly directional site-specific recombination of bacteriophage lambda is tightly regulated by the binding of three different proteins to a complex array of sites. The manner in which these reactions are both stimulated and inhibited by co-operative binding of proteins to specific sites on the P arm ofattP andattR has been elucidated by correlation of nuclease protection with recombination studies of both wild-type and mutant DNAs. In addition to co-operative forces, there is a specific competitive interaction that allows the protein-DNA complex to serve as a “biological switch”. This switch does not depend upon the simple occlusion of DNA binding sites by neighboring proteins; but, rather, the outcome of this competition is dependent on long-range interactions that vary between the higher-order structures ofattP andattR. These higher-order structures are dependent on co-operative interactions involving three proteins binding to five or more sites.