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Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

机译：冷冻电子显微镜观察到的氨酰基-tRNA掺入核糖体中

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摘要

Aminoacyl-tRNAs (aa-tRNAs) are delivered to the ribosome as part of the ternary complex of aa- tRNA, elongation factor Tu (EF-Tu) and GTP. Here, we present a cryo-electron microscopy (cryo-EM) study, at a resolution of similar to9 Angstrom, showing that during the incorporation of the aa- tRNA into the 70S ribosome of Escherichia coli, the flexibility of aa- tRNA allows the initial codon recognition and its accommodation into the ribosomal A site. In addition, a conformational change observed in the GTPase-associated center (GAC) of the ribosomal 50S subunit may provide the mechanism by which the ribosome promotes a relative movement of the aa- tRNA with respect to EF-Tu. This relative rearrangement seems to facilitate codon recognition by the incoming aa- tRNA, and to provide the codon-anticodon recognition-dependent signal for the GTPase activity of EF-Tu. From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome. [References: 44]
机译：氨酰基-tRNA（aa-tRNA）作为aa-tRNA，延伸因子Tu（EF-Tu）和GTP三元复合物的一部分递送至核糖体。在这里，我们进行了一项低温电子显微镜（cryo-EM）研究，其分辨率接近9埃，表明在将atRNA掺入大肠杆菌70S核糖体的过程中，aatRNA的柔性使得初始密码子识别及其在核糖体A位点的调节此外，在核糖体50S亚基的GTPase相关中心（GAC）中观察到的构象变化可能提供了核糖体相对于EF-Tu促进aatRNA相对运动的机制。这种相对重排似乎促进了传入的atRNA的密码子识别，并为EF-Tu的GTPase活性提供了依赖密码子-反密码子识别的信号。从这些新发现中，我们提出了一种机制，可以解释核糖体上mRNA解码期间的事件顺序。 [参考：44]

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