野生型酵母RNA聚合酶II的结构以及Rpb4和Rpb7的定位
Structure of wild-type yeast RNA polymerase II and location of Rpb4 and Rpb7.
作者信息
Jensen G J, Meredith G, Bushnell D A, Kornberg R D
机构信息
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
出版信息
EMBO J. 1998 Apr 15;17(8):2353-8. doi: 10.1093/emboj/17.8.2353.
Abstract
The three-dimensional structure of wild-type yeast RNA polymerase II has been determined at a nominal resolution of 24 A. A difference map between this structure and that of the polymerase lacking subunits Rpb4 and Rpb7 showed these two subunits forming part of the floor of the DNA-binding (active center) cleft, and revealed a slight inward movement of the protein domain surrounding the cleft. Surface plasmon resonance measurements showed that Rpb4 and Rpb7 stabilize a minimal pre-initiation complex containing promoter DNA, TATA box-binding protein (TBP), transcription factor TFIIB and the polymerase. These findings suggest that Rpb4 and Rpb7 play a role in coupling the entry of DNA into the active center cleft to closure of the cleft. Such a role can explain why these subunits are necessary for promoter-specific transcription in vitro and for a normal stress response in vivo.
摘要
野生型酵母RNA聚合酶II的三维结构已在24埃的标称分辨率下确定。该结构与缺乏亚基Rpb4和Rpb7的聚合酶结构之间的差异图显示，这两个亚基构成了DNA结合（活性中心）裂隙底部的一部分，并揭示了围绕裂隙的蛋白质结构域有轻微的向内移动。表面等离子体共振测量表明，Rpb4和Rpb7稳定了一个包含启动子DNA、TATA盒结合蛋白（TBP）、转录因子TFIIB和聚合酶的最小预起始复合物。这些发现表明，Rpb4和Rpb7在将DNA进入活性中心裂隙与裂隙闭合相偶联中发挥作用。这样的作用可以解释为什么这些亚基对于体外启动子特异性转录和体内正常应激反应是必需的。
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