The X-ray crystal structure of RNA polymerase from Archaea
The X-ray crystal structure of RNA polymerase from Archaea
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DOI：
10.1038/nature06844
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发表时间：
2008-03
期刊：
影响因子：
64.8
通讯作者：
A. Hirata;B. J. Klein;K. Murakami
中科院分区：
文献类型：
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作者：
A. Hirata;B. J. Klein;K. Murakami
古细菌中的转录装置可以被描述为真核 RNA 聚合酶 (RNAP) II 对应物的简化版本，包含 RNAPII 样酶以及两个通用转录因子，TATA 结合蛋白 (TBP) 和真核 TFIIB 直系同源物 TFB。人们普遍认为，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件，并且这些见解将有助于分析每种酶的成分，使其能够执行域特异性基因表达。然而，古菌 RNAP 的结构仅限于单个亚基。在这里，我们以 3.4 Å 分辨率报道了来自硫磺硫化叶菌 (Sulfolobus solfataricus) 的古菌 RNAP 的第一个晶体结构，完成了生命所有三个领域的多亚基 RNAP 结构套件。我们还报告了古菌 RNAP 的 D/L 亚复合体的高分辨率（1.76 Å）晶体结构，并提供了任何 RNAP 具有铁硫（Fe-S）簇的第一个实验证据，铁硫簇可能在 RNAP 组装的关键亚基中发挥结构作用。古菌 RNAP 和真核 RNAPII 之间惊人的结构相似性凸显了更简单的古菌 RNAP 作为剖析真核转录分子基础的理想模型系统。
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 TFIIB 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 fromSulfolobus solfataricusat 3.4 Å resolution, completing the suite of multi-subunit RNAP structures from all three domains of life. We also report the high-resolution (at 1.76 Å) 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.