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eIF5B gates the transition from translation initiation to elongation

Author

Listed:
  • Jinfan Wang

    (Stanford University School of Medicine)

  • Alex G. Johnson

    (Stanford University School of Medicine
    Stanford University School of Medicine)

  • Christopher P. Lapointe

    (Stanford University School of Medicine)

  • Junhong Choi

    (Stanford University School of Medicine
    Stanford University)

  • Arjun Prabhakar

    (Stanford University School of Medicine
    Stanford University)

  • Dong-Hua Chen

    (Stanford University School of Medicine)

  • Alexey N. Petrov

    (Stanford University School of Medicine
    Auburn University)

  • Joseph D. Puglisi

    (Stanford University School of Medicine)

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.

Suggested Citation

  • Jinfan Wang & Alex G. Johnson & Christopher P. Lapointe & Junhong Choi & Arjun Prabhakar & Dong-Hua Chen & Alexey N. Petrov & Joseph D. Puglisi, 2019. "eIF5B gates the transition from translation initiation to elongation," Nature, Nature, vol. 573(7775), pages 605-608, September.
  • Handle: RePEc:nat:nature:v:573:y:2019:i:7775:d:10.1038_s41586-019-1561-0
    DOI: 10.1038/s41586-019-1561-0
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    Cited by:

    1. Runlai Hang & Hao Li & Wenjing Liu & Runyu Wang & Hao Hu & Meng Chen & Chenjiang You & Xuemei Chen, 2024. "HOT3/eIF5B1 confers Kozak motif-dependent translational control of photosynthesis-associated nuclear genes for chloroplast biogenesis," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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