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Large ribosomal subunit, eIF5B, Met-tRNAiMet and mRNA cooperate to complete accurate initiation.

By Jinfan Wang, Jing Wang, Byung-Sik Shin, Thomas E. Dever, Joseph D Puglisi, Israel S. Fernández

Posted 31 May 2020
bioRxiv DOI: 10.1101/2020.05.30.125153

Recognition of a start codon by the first aminoacyl-tRNA (Met-tRNAiMet) determines the reading frame of messenger RNA (mRNA) translation by the ribosome. In eukaryotes, the GTPase eIF5B collaborates in the correct positioning of Met tRNAiMet on the ribosome in the later stages of translation initiation, gating entrance into elongation. Leveraging the long residence time of eIF5B on the ribosome recently identified by single-molecule fluorescence measurements, we determined the cryoEM structure of the naturally long-lived ribosome complex with eIF5B and Met-tRNAiMet immediately before transition into elongation. The structure uncovered an unexpected, eukaryotic specific and dynamic fidelity checkpoint implemented by eIF5B in concert with components of the large ribosomal subunit. ### Competing Interest Statement The authors have declared no competing interest.

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