Department of Structural Biology, Stanford School of Medicine, Stanford, CA 94305, USA.
Proc Natl Acad Sci U S A. 2012 Feb 7;109(6):1949-54. doi: 10.1073/pnas.1105266109. Epub 2012 Jan 20.
Structures of complete 10-subunit yeast TFIIH and of a nested set of subcomplexes, containing 5, 6, and 7 subunits, have been determined by electron microscopy (EM) and 3D reconstruction. Consistency among all the structures establishes the location of the "minimal core" subunits (Ssl1, Tfb1, Tfb2, Tfb4, and Tfb5), and additional densities can be specifically attributed to Rad3, Ssl2, and the TFIIK trimer. These results can be further interpreted by placement of previous X-ray structures into the additional densities to give a preliminary picture of the RNA polymerase II preinitiation complex. In this picture, the key catalytic components of TFIIH, the Ssl2 ATPase/helicase and the Kin28 protein kinase are in proximity to their targets, downstream promoter DNA and the RNA polymerase C-terminal domain.
通过电子显微镜(EM)和 3D 重建,已经确定了完整的 10 亚基酵母 TFIIH 以及嵌套的一组亚复合物(包含 5、6 和 7 个亚基)的结构。所有结构的一致性确定了“最小核心”亚基(Ssl1、Tfb1、Tfb2、Tfb4 和 Tfb5)的位置,并且可以将额外的密度特别归因于 Rad3、Ssl2 和 TFIIK 三聚体。通过将先前的 X 射线结构放置到附加密度中,可以进一步解释这些结果,从而给出 RNA 聚合酶 II 起始前复合物的初步图像。在该图像中,TFIIH 的关键催化组件,Ssl2 ATPase/解旋酶和 Kin28 蛋白激酶,与它们的靶标,下游启动子 DNA 和 RNA 聚合酶 C 末端结构域接近。