The X-ray crystal structure of the euryarchaeal RNA polymerase in an open-clamp configuration.
The X-ray crystal structure of the euryarchaeal RNA polymerase in an open-clamp configuration.
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DOI：
10.1038/ncomms6132
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发表时间：
2014-10-14
影响因子：
16.6
通讯作者：
Murakami KS
中科院分区：
文献类型：
--
作者：
Jun SH;Hirata A;Kanai T;Santangelo TJ;Imanaka T;Murakami KS
古细菌的转录装置与真核生物的RNA聚合酶II（Pol II）系统密切相关。细菌RNA聚合酶（RNAP）和Pol II是从一个共同的祖先结构进化而来的，广古细菌RNAP是现存古细菌/真核生物RNAP家族中最简单的成员。在这里，我们报告的第一个晶体结构的euryarchaeal RNAP从热球菌kodakarensis（Tko）。该结构揭示了在Rpo 4/Rpo 7茎存在下，通过这些结构域的协调运动，钳结构域能够摆动远离RNAP的主体。对酵母Pol II和Tko RNAP的更详细的结构-功能分析鉴定了Pol II的结构添加，其对应于Pol II特异性通用转录因子（包括TFIIF、TFIIH和Mediator）的结合位点。这样的比较提供了一个框架，解剖RNAP和这些因素之间的相互作用，在形成的前起始复合物。
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.