剪接体
RNA剪接
生物
内含子
RNA解旋酶A
解旋酶
分子机器
核糖核酸
计算生物学
生物物理学
遗传学
细胞生物学
基因
作者
David Haselbach,I. Komarov,Dmitry E. Agafonov,Klaus Hartmuth,B. Graf,Olexandr Dybkov,Henning Urlaub,Berthold Kastner,Reinhard Lührmann,Holger Stark
出处
期刊:Cell
[Elsevier]
日期:2018-01-01
卷期号:172 (3): 454-464.e11
被引量:177
标识
DOI:10.1016/j.cell.2018.01.010
摘要
The spliceosome is a highly dynamic macromolecular complex that precisely excises introns from pre-mRNA. Here we report the cryo-EM 3D structure of the human Bact spliceosome at 3.4 Å resolution. In the Bact state, the spliceosome is activated but not catalytically primed, so that it is functionally blocked prior to the first catalytic step of splicing. The spliceosomal core is similar to the yeast Bact spliceosome; important differences include the presence of the RNA helicase aquarius and peptidyl prolyl isomerases. To examine the overall dynamic behavior of the purified spliceosome, we developed a principal component analysis-based approach. Calculating the energy landscape revealed eight major conformational states, which we refined to higher resolution. Conformational differences of the highly flexible structural components between these eight states reveal how spliceosomal components contribute to the assembly of the spliceosome, allowing it to generate a dynamic interaction network required for its subsequent catalytic activation.
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