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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >tRNA dynamics on the ribosome during translation.
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tRNA dynamics on the ribosome during translation.

机译：翻译过程中核糖体上的tRNA动态。

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摘要

Using single-molecule fluorescence spectroscopy, time-resolved conformational changes between fluorescently labeled tRNA have been characterized within surface-immobilized ribosomes proceeding through a complete cycle of translation elongation. Fluorescence resonance energy transfer was used to observe aminoacyl-tRNA (aa-tRNA) stably accommodating into the aminoacyl site (A site) of the ribosome via a multistep, elongation factor-Tu dependent process. Subsequently, tRNA molecules, bound at the peptidyl site and A site, fluctuate between two configurations assigned as classical and hybrid states. The lifetime of classical and hybrid states, measured for complexes carrying aa-tRNA and peptidyl-tRNA at the A site, shows that peptide bond formation decreases the lifetime of the classical-state tRNA configuration by approximately 6-fold. These data suggest that the growing peptide chain plays a role in modulating fluctuations between hybrid and classical states. Single-molecule fluorescence resonance energytransfer was also used to observe aa-tRNA accommodation coupled with elongation factor G-mediated translocation. Dynamic rearrangements in tRNA configuration are also observed subsequent to the translocation reaction. This work underscores the importance of dynamics in ribosome function and demonstrates single-particle enzymology in a system of more than two components.
机译：使用单分子荧光光谱法，已在表面固定的核糖体中进行了荧光标记的tRNA之间的时间分辨构象变化，并经历了翻译延伸的完整循环。荧光共振能量转移用于观察氨基酰基-tRNA（aa-tRNA）通过多步伸长因子-Tu依赖性过程稳定地容纳在核糖体的氨基酰基位点（A位点）中。随后，结合在肽基位点和A位点上的tRNA分子在分配为经典状态和杂交状态的两种构型之间波动。对在A位点携带aa-tRNA和肽基tRNA的复合物测量的经典状态和杂种状态的寿命表明，肽键的形成将经典状态tRNA构型的寿命降低了约6倍。这些数据表明，不断增长的肽链在调节杂合态和经典态之间的波动中发挥作用。还使用单分子荧光共振能量转移来观察aa-tRNA调节与延伸因子G介导的易位。易位反应后，还观察到了tRNA构型的动态重排。这项工作强调了核糖体功能动力学的重要性，并证明了具有两个以上组成部分的系统中的单颗粒酶学。

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