Structural basis for the transition from translation initiation to elongation by an 80S-eIF5B complex

Jinfan Wang, Jing Wang, Byung-Sik Shin, Joo-Ran Kim, Thomas E. Dever (), Joseph D. Puglisi () and Israel S. Fernández ()
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Jinfan Wang: Stanford University School of Medicine
Jing Wang: Columbia University
Byung-Sik Shin: Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH
Joo-Ran Kim: Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH
Thomas E. Dever: Eunice Kennedy Shriver National Institute of Child Health and Human Development, NIH
Joseph D. Puglisi: Stanford University School of Medicine
Israel S. Fernández: Columbia University

Nature Communications, 2020, vol. 11, issue 1, 1-8

Abstract: Abstract Recognition of a start codon by the initiator aminoacyl-tRNA determines the reading frame of messenger RNA (mRNA) translation by the ribosome. In eukaryotes, the GTPase eIF5B collaborates in the correct positioning of the initiator 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 determine the cryoEM structure of the naturally long-lived ribosome complex with eIF5B and Met-tRNAiMet immediately before transition into elongation. The structure uncovers an unexpected, eukaryotic specific and dynamic fidelity checkpoint implemented by eIF5B in concert with components of the large ribosomal subunit.

Date: 2020
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DOI: 10.1038/s41467-020-18829-3

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