eIF5B gates the transition from translation initiation to elongation

Jinfan Wang, Alex G. Johnson, Christopher P. Lapointe, Junhong Choi, Arjun Prabhakar, Dong-Hua Chen, Alexey N. Petrov and Joseph D. Puglisi ()
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Jinfan Wang: Stanford University School of Medicine
Alex G. Johnson: Stanford University School of Medicine
Christopher P. Lapointe: Stanford University School of Medicine
Junhong Choi: Stanford University School of Medicine
Arjun Prabhakar: Stanford University School of Medicine
Dong-Hua Chen: Stanford University School of Medicine
Alexey N. Petrov: Stanford University School of Medicine
Joseph D. Puglisi: Stanford University School of Medicine

Nature, 2019, vol. 573, issue 7775, 605-608

Abstract: Abstract Translation initiation determines both the quantity and identity of the protein that is encoded in an mRNA by establishing the reading frame for protein synthesis. In eukaryotic cells, numerous translation initiation factors prepare ribosomes for polypeptide synthesis; however, the underlying dynamics of this process remain unclear1,2. A central question is how eukaryotic ribosomes transition from translation initiation to elongation. Here we use in vitro single-molecule fluorescence microscopy approaches in a purified yeast Saccharomyces cerevisiae translation system to monitor directly, in real time, the pathways of late translation initiation and the transition to elongation. This transition was slower in our eukaryotic system than that reported for Escherichia coli3–5. The slow entry to elongation was defined by a long residence time of eukaryotic initiation factor 5B (eIF5B) on the 80S ribosome after the joining of individual ribosomal subunits—a process that is catalysed by this universally conserved initiation factor. Inhibition of the GTPase activity of eIF5B after the joining of ribosomal subunits prevented the dissociation of eIF5B from the 80S complex, thereby preventing elongation. Our findings illustrate how the dissociation of eIF5B serves as a kinetic checkpoint for the transition from initiation to elongation, and how its release may be governed by a change in the conformation of the ribosome complex that triggers GTP hydrolysis.

Date: 2019
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DOI: 10.1038/s41586-019-1561-0

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