Journal
NUCLEIC ACIDS RESEARCH
Volume 45, Issue 19, Pages 10948-10968Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkx805
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Funding
- Wellcome Trust [090812/B/09/Z]
- Czech Science Foundation [GA17-06238S]
- Agence Nationale de la Recherche [LabEx: ANR-10-LABX-0036_NETRNA, ANR-14-ACHN-0024 CryoEM80S]
- Wellcome Trust
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Protein synthesis is mediated via numerous molecules including the ribosome, mRNA, tRNAs, as well as translation initiation, elongation and release factors. Some of these factors play several roles throughout the entire process to ensure proper assembly of the preinitiation complex on the right mRNA, accurate selection of the initiation codon, errorless production of the encoded polypeptide and its proper termination. Perhaps, the most intriguing of these multitasking factors is the eukaryotic initiation factor eIF3. Recent evidence strongly suggests that this factor, which coordinates the progress of most of the initiation steps, does not come off the initiation complex upon subunit joining, but instead it remains bound to 80S ribosomes and gradually falls off during the first few elongation cycles to: (1) promote resumption of scanning on the same mRNA molecule for reinitiation downstream-in case of translation of upstream ORFs short enough to preserve eIF3 bound; or (2) come back during termination on long ORFs to fine tune its fidelity or, if signaled, promote programmed stop codon readthrough. Here, we unite recent structural views of the eIF3-40S complex and discus all known eIF3 roles to provide a broad picture of the eIF3' s impact on translational control in eukaryotic cells.
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