ArticleNucleic acids research2016
Attachment of ribosomal complexes and retrograde scanning during initiation on the Halastavi árva virus IRES.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Guidelines for minimal reporting requirements, design and interpretation of experiments involving the use of eukaryotic dual gene expression reporters (MINDR).Nature structural & molecular biology · 2025Review
- Translation of Overlapping Open Reading Frames Promoted by Type 2 IRESs in Avian Calicivirus Genomes.Viruses · 2024Article
- Host-like RNA Elements Regulate Virus Translation.Viruses · 2024Review
- The molecular basis of translation initiation and its regulation in eukaryotes.Nature reviews. Molecular cell biology · 2024Review
- Preinitiation Complex Loading onto mRNAs with Long versus Short 5' TLs.International journal of molecular sciences · 2022Article
- Review
- Bi-directional ribosome scanning controls the stringency of start codon selection.Nature communications · 2021Article
- Non-Canonical Translation Initiation Mechanisms Employed by Eukaryotic Viral mRNAs.Biochemistry. Biokhimiia · 2021Review
- A translation enhancer element from black beetle virus engages yeast eIF4G1 to drive cap-independent translation initiation.Scientific reports · 2021Article
- The Halastavi árva Virus Intergenic Region IRES Promotes Translation by the Simplest Possible Initiation Mechanism.Cell reports · 2020Article
- Dissemination of Internal Ribosomal Entry Sites (IRES) Between Viruses by Horizontal Gene Transfer.Viruses · 2020Review
- In Vitro Characterization of the Activity of the Mammalian RNA Exosome on mRNAs in Ribosomal Translation Complexes.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Migration of Small Ribosomal Subunits on the 5' Untranslated Regions of Capped Messenger RNA.International journal of molecular sciences · 2019Article
- IRES-dependent ribosome repositioning directs translation of a +1 overlapping ORF that enhances viral infection.Nucleic acids research · 2018Article
- Distinct roles for the IIId2 sub-domain in pestivirus and picornavirus internal ribosome entry sites.Nucleic acids research · 2017Article
- The IRES5'UTR of the dicistrovirus cricket paralysis virus is a type III IRES containing an essential pseudoknot structure.Nucleic acids research · 2017Article
- Two ribosome recruitment sites direct multiple translation events within HIV1 Gag open reading frame.Nucleic acids research · 2017Article
- A researcher's guide to the galaxy of IRESs.Cellular and molecular life sciences : CMLS · 2017Review
- Insights into Structural and Mechanistic Features of Viral IRES Elements.Frontiers in microbiology · 2017Review
- Toward the mechanism of eIF4F-mediated ribosomal attachment to mammalian capped mRNAs.Genes & development · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Halastavi árva virus (HalV) has a positive-sense RNA genome, with an 827 nt-long 5' UTR and an intergenic region separating two open reading frames. Whereas the encoded proteins are most homologous to Dicistrovirus polyproteins, its 5' UTR is distinct. Here, we report that the HalV 5' UTR comprises small stem-loop domains separated by long single-stranded areas and a large A-rich unstructured region surrounding the initiation codon AUG828, and possesses cross-kingdom internal ribosome entry site (IRES) activity. In contrast to most viral IRESs, it does not depend on structural integrity and specific interaction of a structured element with a translational component, and is instead determined by the unstructured region flanking AUG828. eIF2, eIF3, eIF1 and eIF1A promote efficient 48S initiation complex formation at AUG828, which is reduced ∼5-fold on omission of eIF1 and eIF1A. Initiation involves direct attachment of 43S preinitiation complexes within a short window at or immediately downstream of AUG828. 40S and eIF3 are sufficient for initial binding. After attachment, 43S complexes undergo retrograde scanning, strongly dependent on eIF1 and eIF1A. eIF4A/eIF4G stimulated initiation only at low temperatures or on mutants, in which areas surrounding AUG828 had been replaced by heterologous sequences. However, they strongly promoted initiation at AUG872, yielding a proline-rich oligopeptide.
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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.