Structural studies of Escherichia coli RNA polymerase.
Structural studies of Escherichia coli RNA polymerase.
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大肠杆菌 RNA 聚合酶的结构研究。
DOI：
10.1101/sqb.1998.63.269
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
Zhang,G
中科院分区：
文献类型：
--
作者：
Darst,SA;Polyakov,A;Richter,C;Zhang,G
负染晶体中RNA聚合酶的低分辨结构。到目前为止，多亚基细胞RNAP的结构来自电子显微镜和负染色晶体的图像处理，导致蛋白质在重金属包埋介质(如醋酸铀酰)中留下的凹陷或铸型的图像。大肠杆菌RNAP全酶的低分辨率、三维结构(Darst等人1989)和酵母RNAPs II(Darst等人)。1991)和I(Schultz et al.1993年)，通过与入射电子束成不同角度倾斜的负染二维晶体的电子显微镜来确定(Amos等人)。1982年)。我们随后的大肠杆菌核心RNAP的结构，它缺乏启动子特异的σ亚基，与大肠杆菌RNAP全酶相比显示出显著的构象变化，但类似于酵母RNAP II(Polyakov等人)。1995年)。尽管每个结构都包含一个拇指状突起，围绕着直径约为25？的凹槽或通道，这是适当的
Low-resolution structures of RNA polymerases from negatively stained crystals. Structures to date of the multisubunit cellular RNAPs have come from electron microscopy and image processing of negatively stained crystals, resulting in an image of the depression or cast that the protein leaves in a heavy-metal embedding medium such as uranyl acetate. Low-resolution, three-dimensional structures of E. coli RNAP holoenzyme (Darst et al. 1989), and yeast RNAPs II (Darst et al. 1991) and I (Schultz et al. 1993), were determined by electron microscopy of negatively stained two-dimensional crystals tilted at various angles to the incident electron beam (Amos et al. 1982). Our subsequent structure of E. coli core RNAP, which lacks the promoter-specific σ-subunit, revealed dramatic conformational changes compared with the E. coli RNAP holoenzyme but resembled yeast RNAP II (Polyakov et al. 1995). Although each structure contains a thumb-like projection surrounding a groove or channel about 25 Å in diameter, which is the appropriate