由DNA弯曲蛋白IHF和λ整合酶的两个结构域产生的DNA环化
DNA looping generated by DNA bending protein IHF and the two domains of lambda integrase.
作者信息
Moitoso de Vargas L, Kim S, Landy A
机构信息
Division of Biology and Medicine, Brown University, Providence, RI 02912.
出版信息
Science. 1989 Jun 23;244(4911):1457-61. doi: 10.1126/science.2544029.
Abstract
The multiprotein-DNA complexes that participate in bacteriophage lambda site-specific recombination were used to study the combined effect of protein-induced bending and protein-mediated looping of DNA. The protein integrase (Int) is a monomer with two autonomous DNA binding domains of different sequence specificity. Stimulation of Int binding and cleavage at the low affinity core-type DNA sites required interactions with the high affinity arm-type sites and depended on simultaneous binding of the sequence-specific DNA bending protein IHF (integration host factor). The bivalent DNA binding protein is positioned at high affinity sites and directed, by a DNA bending protein, to interactions with distant lower affinity sites. Assembly of this complex is independent of protein-protein interactions.
摘要
参与噬菌体λ位点特异性重组的多蛋白-DNA复合物被用于研究蛋白质诱导的DNA弯曲和蛋白质介导的DNA环化的联合效应。蛋白质整合酶（Int）是一种单体，具有两个序列特异性不同的自主DNA结合结构域。在低亲和力核心型DNA位点刺激Int结合和切割需要与高亲和力臂型位点相互作用，并依赖于序列特异性DNA弯曲蛋白IHF（整合宿主因子）的同时结合。二价DNA结合蛋白定位在高亲和力位点，并由一种DNA弯曲蛋白引导，与远处的低亲和力位点相互作用。该复合物的组装不依赖于蛋白质-蛋白质相互作用。
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