ArticleJournal of molecular biology2010
Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunit.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 33 citations in OpenAlex.
- Integrating rna structure and protein interactions to uncover the mechanisms of viral and cellular ires function.Biology direct · 2025Article
- Article
- RNA-based translation activators for targeted gene upregulation.Nature communications · 2023Article
- eIF3 Interacts with Selenoprotein mRNAs.Biomolecules · 2022Article
- Article
- Unlike for cellular mRNAs and other viral internal ribosome entry sites (IRESs), the eIF3 subunit e is not required for the translational activity of the HCV IRES.The Journal of biological chemistry · 2020Article
- Eukaryotic initiation factor (eIF) 3 mediates Barley Yellow Dwarf Viral mRNA 3'-5' UTR interactions and 40S ribosomal subunit binding to facilitate cap-independent translation.Nucleic acids research · 2019Article
- Alternative mechanisms of translation initiation: An emerging dynamic regulator of the proteome in health and disease.Life sciences · 2018Review
- Heterogeneity and specialized functions of translation machinery: from genes to organisms.Nature reviews. Genetics · 2018Review
- microRNAs stimulate translation initiation mediated by HCV-like IRESes.Nucleic acids research · 2017Article
- Human eIF3: from 'blobology' to biological insight.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Dynamics of IRES-mediated translation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Screening and analysis on the protein interaction of the protein VP7 in grass carp reovirus.Virus genes · 2015Article
- Functional and biochemical characterization of human eukaryotic translation initiation factor 3 in living cells.Molecular and cellular biology · 2014Article
- Phosphorylation stoichiometries of human eukaryotic initiation factors.International journal of molecular sciences · 2014Article
- Two RNA-binding motifs in eIF3 direct HCV IRES-dependent translation.Nucleic acids research · 2013Article
- The eukaryotic translation initiation factor 3 subunit L protein interacts with Flavivirus NS5 and may modulate yellow fever virus replication.Virology journal · 2013Article
- Architecture of human translation initiation factor 3.Structure (London, England : 1993) · 2013Article
- Novel mass spectrometric method for phosphorylation quantification using cerium oxide nanoparticles and tandem mass tags.Analytical chemistry · 2012Article
- Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3).Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Translation of the hepatitis C virus (HCV) genomic RNA initiates from an internal ribosome entry site (IRES) in its 5' untranslated region and requires a minimal subset of translation initiation factors to occur, namely eukaryotic initiation factor (eIF) 2 and eIF3. Low-resolution structural information has revealed how the HCV IRES RNA binds human eIF3 and the 40S ribosomal subunit and positions the start codon for initiation. However, the exact nature of the interactions between the HCV IRES RNA and the translational machinery remains unknown. Using limited proteolysis and mass spectrometry, we show that distinct regions of human eIF3 are sufficient for binding to the HCV IRES RNA and the 40S subunit. Notably, the eIF3 subunit eIF3b is protected by HCV IRES RNA binding, yet is exposed in the complex when compared to subunits eIF3e, eIF3f, eIF3h, and eIF3l. Limited proteolysis reveals that eIF3 binding to the 40S ribosomal subunit occurs through many redundant interactions that can compensate for each other. These data suggest how the HCV IRES binds to specific regions of eIF3 to target the translational machinery to the viral genomic RNA and provide a framework for modeling the architecture of intact human eIF3.
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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.