ArticleMolecular and cellular biology1998
Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.
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Who cites it
88 citing papers in PubMed, 185 citations in OpenAlex.
- eIF1 and eIF5 dynamically control translation start site fidelity.Nature structural & molecular biology · 2025Article
- Cellular translational enhancer elements that recruit eukaryotic initiation factor 3.RNA (New York, N.Y.) · 2025Article
- A dynamic compositional equilibrium governs mRNA recognition by eIF3.bioRxiv : the preprint server for biology · 2024Article
- Identification of acetic acid sensitive strains through biosensor-based screening of a Saccharomyces cerevisiae CRISPRi library.Microbial cell factories · 2022Article
- The PCI domains are "winged" HEAT domains.PloS one · 2022Article
- Reprogramming mRNA Expression in Response to Defect in RNA Polymerase III Assembly in the YeastInternational journal of molecular sciences · 2021Article
- eIF3a Destabilization and TDP-43 Alter Dynamics of Heat-Induced Stress Granules.International journal of molecular sciences · 2021Article
- Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.Cell reports · 2020Article
- DENR promotes translation reinitiation via ribosome recycling to drive expression of oncogenes including ATF4.Nature communications · 2020Article
- Selective Translation Complex Profiling Reveals Staged Initiation and Co-translational Assembly of Initiation Factor Complexes.Molecular cell · 2020Article
- Binding of eIF3 in complex with eIF5 and eIF1 to the 40S ribosomal subunit is accompanied by dramatic structural changes.Nucleic acids research · 2019Article
- An aggregation-prone mutant of eIF3a forms reversible assemblies escaping spatial control in exponentially growing yeast cells.Current genetics · 2019Article
- Reconstitution and analyses of RNA interactions with eukaryotic translation initiation factors and ribosomal preinitiation complexes.Methods (San Diego, Calif.) · 2019Article
- Alternative mechanisms of translation initiation: An emerging dynamic regulator of the proteome in health and disease.Life sciences · 2018Review
- Structure of a human cap-dependent 48S translation pre-initiation complex.Nucleic acids research · 2018Article
- The Biological Roles of Translation Initiation Factor 3b.International journal of biological sciences · 2018Review
- Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle.Nucleic acids research · 2017Article
- Human eIF3: from 'blobology' to biological insight.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.Cell reports · 2017Article
- Human eIF3b and eIF3a serve as the nucleation core for the assembly of eIF3 into two interconnected modules: the yeast-like core and the octamer.Nucleic acids research · 2016Article
28 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Only five of the nine subunits of human eukaryotic translation initiation factor 3 (eIF3) have recognizable homologs encoded in the Saccharomyces cerevisiae genome, and only two of these (Prt1p and Tif34p) were identified previously as subunits of yeast eIF3. We purified a polyhistidine-tagged form of Prt1p (His-Prt1p) by Ni2+ affinity and gel filtration chromatography and obtained a complex of approximately 600 kDa composed of six polypeptides whose copurification was completely dependent on the polyhistidine tag on His-Prt1p. All five polypeptides associated with His-Prt1p were identified by mass spectrometry, and four were found to be the other putative homologs of human eIF3 subunits encoded in S. cerevisiae: YBR079c/Tif32p, Nip1p, Tif34p, and YDR429c/Tif35p. The fifth Prt1p-associated protein was eIF5, an initiation factor not previously known to interact with eIF3. The purified complex could rescue Met-tRNAiMet binding to 40S ribosomes in defective extracts from a prt1 mutant or extracts from which Nip1p had been depleted, indicating that it possesses a known biochemical activity of eIF3. These findings suggest that Tif32p, Nip1p, Prt1p, Tif34p, and Tif35p comprise an eIF3 core complex, conserved between yeast and mammals, that stably interacts with eIF5. Nip1p bound to eIF5 in yeast two-hybrid and in vitro protein binding assays. Interestingly, Sui1p also interacts with Nip1p, and both eIF5 and Sui1p have been implicated in accurate recognition of the AUG start codon. Thus, eIF5 and Sui1p may be recruited to the 40S ribosomes through physical interactions with the Nip1p subunit of eIF3.
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