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The X-ray crystal structure of RNA polymerase from Archaea

机译：古细菌RNA聚合酶的X射线晶体结构

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摘要

The transcription apparatus in Archaea can be described as a simplified version of its eukaryotic RNA polymerase (RNAP) II counterpart, comprising an RNAPII-like enzyme as well as two general transcription factors, the TATA-binding protein (TBP) and the eukaryotic TFHB orthologue TFB. It has been widely understood that precise comparisons of cellular RNAP crystal structures could reveal structural elements common to all enzymes and that these insights would be useful in analysing components of each enzyme that enable it to perform domain-specific gene expression. However, the structure of archaeal RNAP has been limited to individual subunits. Here we report the first crystal structure of the archaeal RNAP from Sulfolobus solfataricus at 3.4 A resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 A) crystal structure of the D/L subcomplex of archaeal RNAP and provide the first experimental evidence of any RNAP possessing an iron-sulphur (Fe-S) cluster, which may play a structural role in a key subunit of RNAP assembly. The striking structural similarity between archaeal RNAP and eukaryotic RNAPII highlights the simpler archaeal RNAP as an ideal model system for dissecting the molecular basis of eukaryotic transcription.
机译：古细菌中的转录装置可描述为其真核RNA聚合酶（RNAP）II对应物的简化版本，包括RNAPII样酶以及两种通用转录因子，即TATA结合蛋白（TBP）和真核TFHB直系同源物TFB。众所周知，细胞RNAP晶体结构的精确比较可以揭示所有酶共有的结构元素，这些见解将有助于分析每种酶的成分，从而使其能够执行结构域特异性基因表达。但是，古细菌RNAP的结构仅限于单个亚基。在这里，我们以3.4 A的分辨率报告了来自Sulfolobus solfataricus的古细菌RNAP的第一个晶体结构，从而完成了生活中所有三个域的多亚基RNAP结构套件。我们还报告了古细菌RNAP的D / L亚复合物的高分辨率（1.76 A）晶体结构，并提供了任何具有铁硫（Fe-S）簇的RNAP的第一个实验证据，这可能起结构​​性作用在RNAP装配的关键亚基中。古细菌RNAP和真核RNAPII之间惊人的结构相似性凸显了较简单的古细菌RNAP，是解剖真核转录分子基础的理想模型系统。

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