Robinson Philip J, Trnka Michael J, Bushnell David A, Davis Ralph E, Mattei Pierre-Jean, Burlingame Alma L, Kornberg Roger D
Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Cell. 2016 Sep 8;166(6):1411-1422.e16. doi: 10.1016/j.cell.2016.08.050.
A complete, 52-protein, 2.5 million dalton, Mediator-RNA polymerase II pre-initiation complex (Med-PIC) was assembled and analyzed by cryo-electron microscopy and by chemical cross-linking and mass spectrometry. The resulting complete Med-PIC structure reveals two components of functional significance, absent from previous structures, a protein kinase complex and the Mediator-activator interaction region. It thereby shows how the kinase and its target, the C-terminal domain of the polymerase, control Med-PIC interaction and transcription.
通过冷冻电子显微镜以及化学交联和质谱分析，组装并分析了一个完整的、由52种蛋白质组成、分子量为250万道尔顿的中介体 - RNA聚合酶II预起始复合物（Med-PIC）。所得的完整Med-PIC结构揭示了之前结构中不存在的两个具有功能意义的组分，即一个蛋白激酶复合物和中介体 - 激活剂相互作用区域。由此展示了激酶及其靶点——聚合酶的C末端结构域如何控制Med-PIC相互作用和转录。
