Jun Sung-Hoon, Hirata Akira, Kanai Tamotsu, Santangelo Thomas J, Imanaka Tadayuki, Murakami Katsuhiko S
Department of Biochemistry and Molecular Biology, The Center for RNA Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
1] Department of Biochemistry and Molecular Biology, The Center for RNA Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA [2] Department of Materials Science and Biotechnology, Graduate School of Science and Engineering, Ehime University, Matsuyama, Ehime 790-8577, Japan.
Nat Commun. 2014 Oct 14;5:5132. doi: 10.1038/ncomms6132.
The archaeal transcription apparatus is closely related to the eukaryotic RNA polymerase II (Pol II) system. Archaeal RNA polymerase (RNAP) and Pol II evolved from a common ancestral structure and the euryarchaeal RNAP is the simplest member of the extant archaeal-eukaryotic RNAP family. Here we report the first crystal structure of euryarchaeal RNAP from Thermococcus kodakarensis (Tko). This structure reveals that the clamp domain is able to swing away from the main body of RNAP in the presence of the Rpo4/Rpo7 stalk by coordinated movements of these domains. More detailed structure-function analysis of yeast Pol II and Tko RNAP identifies structural additions to Pol II that correspond to the binding sites of Pol II-specific general transcription factors including TFIIF, TFIIH and Mediator. Such comparisons provide a framework for dissecting interactions between RNAP and these factors during formation of the pre-initiation complex.
古细菌转录装置与真核生物RNA聚合酶II（Pol II）系统密切相关。古细菌RNA聚合酶（RNAP）和Pol II由共同的祖先结构进化而来，广古菌RNAP是现存古细菌-真核生物RNAP家族中最简单的成员。在此，我们报道了来自嗜热栖热菌（Tko）的广古菌RNAP的首个晶体结构。该结构表明，在Rpo4/Rpo7柄存在的情况下，钳结构域能够通过这些结构域的协同运动从RNAP主体摆动开。对酵母Pol II和Tko RNAP进行更详细的结构-功能分析，确定了Pol II的结构添加物，这些添加物对应于Pol II特异性通用转录因子（包括TFIIF、TFIIH和中介体）的结合位点。此类比较为剖析预起始复合物形成过程中RNAP与这些因子之间的相互作用提供了一个框架。
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