ArticleThe EMBO journal2008
eIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II.
Article in The EMBO journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed, 150 citations in OpenAlex.
- Distribution and structural diversity of type IV internal ribosome entry sites.RNA (New York, N.Y.) · 2026Article
- The mechanism of ribosomal recruitment during translation initiation on the Type 2 encephalomyocarditis virus IRES.The EMBO journal · 2026Article
- Eukaryotic translation initiation factor 4F: functional properties and physiological role.Nucleic acids research · 2025Review
- Review
- Predicting cellular adaptation proteins dependent on eIF2α regulation under stress conditions: Physiological and pathophysiological implications in neuronal function.Computational and structural biotechnology journal · 2025Article
- Host-like RNA Elements Regulate Virus Translation.Viruses · 2024Review
- Article
- The intrinsically disordered region of eIF5B stimulates IRES usage and nucleates biological granule formation.Cell reports · 2023Article
- The enterovirus genome can be translated in an IRES-independent manner that requires the initiation factors eIF2A/eIF2D.PLoS biology · 2023Article
- eIF3j inhibits translation of a subset of circular RNAs in eukaryotic cells.Nucleic acids research · 2022Article
- Molecular architecture of 40S translation initiation complexes on the hepatitis C virus IRES.The EMBO journal · 2022Article
- Role of aIF5B in archaeal translation initiation.Nucleic acids research · 2022Article
- Incorporation and Utility of a Responsive Ribonucleoside Analogue in Probing the Conformation of a Viral RNA Motif by Fluorescence andChembiochem : a European journal of chemical biology · 2022Article
- Horizontal gene transfer as a mechanism for the promiscuous acquisition of distinct classes of IRES by avian caliciviruses.Nucleic acids research · 2022Article
- eIF2A-knockout mice reveal decreased life span and metabolic syndrome.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Non-Canonical Translation Initiation Mechanisms Employed by Eukaryotic Viral mRNAs.Biochemistry. Biokhimiia · 2021Review
- Mechanisms of repeat-associated non-AUG translation in neurological microsatellite expansion disorders.Biochemical Society transactions · 2021Review
- Established and Emerging Regulatory Roles of Eukaryotic Translation Initiation Factor 5B (eIF5B).Frontiers in genetics · 2021Review
- Depletion of eukaryotic initiation factor 5B (eIF5B) reprograms the cellular transcriptome and leads to activation of endoplasmic reticulum (ER) stress and c-Jun N-terminal kinase (JNK).Cell stress & chaperones · 2021Article
- Dissemination of Internal Ribosomal Entry Sites (IRES) Between Viruses by Horizontal Gene Transfer.Viruses · 2020Review
43 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Specific interactions of the classical swine fever virus internal ribosomal entry site (IRES) with 40S ribosomal subunits and eukaryotic translation initiation factor (eIF)3 enable 43S preinitiation complexes containing eIF3 and eIF2-GTP-Met-tRNA(iMet) to bind directly to the initiation codon, yielding 48S initiation complexes. We report that eIF5B or eIF5B/eIF3 also promote Met-tRNA(iMet) binding to IRES-40S complexes, forming 48S complexes that can assemble elongation-competent ribosomes. Although 48S complexes assembled both by eIF2/eIF3- and eIF5B/eIF3-mediated Met-tRNA(iMet) recruitment were destabilized by eIF1, dissociation of 48S complexes formed with eIF2 could be out-competed by efficient subunit joining. Deletion of IRES domain II, which is responsible for conformational changes induced in 40S subunits by IRES binding, eliminated the sensitivity of 48S complexes assembled by eIF2/eIF3- and eIF5B/eIF3-mediated mechanisms to eIF1-induced destabilization. However, 48S complexes formed by the eIF5B/eIF3-mediated mechanism on the truncated IRES could not undergo efficient subunit joining, as reported previously for analogous complexes assembled with eIF2, indicating that domain II is essential for general conformational changes in 48S complexes, irrespective of how they were assembled, that are required for eIF5-induced hydrolysis of eIF2-bound GTP and/or subunit joining.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.