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Snapshots of pre-rRNA structural flexibility reveal eukaryotic 40S assembly dynamics at nucleotide resolution

机译:前rRNA结构灵活性的快照显示了核苷酸分辨率下的真核40S装配动力学

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摘要

Ribosome assembly in eukaryotes involves the activity of hundreds of assembly factors that direct the hierarchical assembly of ribosomal proteins and numerous ribosomal RNA folding steps. However, detailed insights into the function of assembly factors and ribosomal RNA folding events are lacking. To address this, we have developed ChemModSeq, a method that combines structure probing, high-throughput sequencing and statistical modeling, to quantitatively measure RNA structural rearrangements during the assembly of macromolecular complexes. By applying ChemModSeq to purified 40S assembly intermediates we obtained nucleotide-resolution maps of ribosomal RNA flexibility revealing structurally distinct assembly intermediates and mechanistic insights into assembly dynamics not readily observed in cryo-electron microscopy reconstructions. We show that RNA restructuring events coincide with the release of assembly factors and predict that completion of the head domain is required before the Rio1 kinase enters the assembly pathway. Collectively, our results suggest that 40S assembly factors regulate the timely incorporation of ribosomal proteins by delaying specific folding steps in the 3′ major domain of the 20S pre-ribosomal RNA.
机译:真核生物中的核糖体组装涉及数百个组装因子的活性,这些因子指导核糖体蛋白的分级组装和许多核糖体RNA折叠步骤。但是,缺乏对装配因子和核糖体RNA折叠事件的功能的深入了解。为了解决这个问题,我们开发了ChemModSeq,一种结合结构探测,高通量测序和统计建模的方法,可以在大分子复合物组装过程中定量测量RNA结构重排。通过将ChemModSeq应用到纯化的40S组装中间体上,我们获得了核糖体RNA柔性的核苷酸分辨率图谱,揭示了结构独特的组装中间体和对组装动力学的力学见解,在冷冻电子显微镜重建中不容易观察到。我们显示RNA重组事件与装配因子的释放相吻合,并预测在Rio1激酶进入装配路径之前需要完成头部结构域。总的来说,我们的结果表明40S装配因子通过延迟20S核糖体RNA的3'主要结构域中的特定折叠步骤来调节核糖体蛋白的及时掺入。

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