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TitleeIF5B gates the transition from translation initiation to elongation.
Journal, issue, pagesNature, Vol. 573, Issue 7775, Page 605-608, Year 2019
Publish dateSep 18, 2019
AuthorsJinfan Wang / Alex G Johnson / Christopher P Lapointe / Junhong Choi / Arjun Prabhakar / Dong-Hua Chen / Alexey N Petrov / Joseph D Puglisi /
PubMed AbstractTranslation 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 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 unclear. 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 coli. 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.
External linksNature / PubMed:31534220 / PubMed Central
MethodsEM (single particle)
Resolution8.4 - 10.1 Å
Structure data

EMDB-20324:
Structure of a partial yeast post-scanning 48S preinitiation complex
Method: EM (single particle) / Resolution: 9.9 Å

EMDB-20325:
Cryo-EM structure of yeast eIF5B-bound 80S initiation complex (80S IC)
Method: EM (single particle) / Resolution: 8.4 Å

EMDB-20326:
Cryo-EM structure of yeast elongation-competent 80S complex (80S EC)
Method: EM (single particle) / Resolution: 10.1 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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