ArticleProceedings of the National Academy of Sciences of the United States of America2015
Global shape mimicry of tRNA within a viral internal ribosome entry site mediates translational reading frame selection.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 33 citations in OpenAlex.
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- Genetic mechanisms underlying the structural elaboration and dissemination of viral internal ribosomal entry sites.Nucleic acids research · 2026Article
- Structural studies of nedicistrovirus IRES-driven, initiation factor-independent translation shed light on key steps of eukaryotic translation elongation.Nucleic acids research · 2026Article
- Structural Studies of Nedicistrovirus IRES-Driven, Initiation Factor-independent Translation Shed Light on Key Steps of Eukaryotic Translation Elongation.bioRxiv : the preprint server for biology · 2025Article
- A conserved viral RNA fold enables nuclease resistance across kingdoms of life.Nucleic acids research · 2025Article
- Discovery of functional factorless internal ribosome entry site-like structures through virome mining.PLoS pathogens · 2025Article
- Gut-binding peptides as potential tools to reduce virus binding to honey bee gut surface proteins.Applied and environmental microbiology · 2025Article
- Structural basis of MALAT1 RNA maturation and mascRNA biogenesis.Nature structural & molecular biology · 2024Article
- tRNA renovatio: Rebirth through fragmentation.Molecular cell · 2023Review
- The bacterial yjdF riboswitch regulates translation through its tRNA-like fold.The Journal of biological chemistry · 2022Article
- The Hinge Region of the Israeli Acute Paralysis Virus Internal Ribosome Entry Site Directs Ribosomal Positioning, Translational Activity, and Virus Infection.Journal of virology · 2022Article
- Binding of a viral IRES to the 40S subunit occurs in two successive steps mediated by eS25.Nucleic acids research · 2020Article
- The nature of the purine at position 34 in tRNAs of 4-codon boxes is correlated with nucleotides at positions 32 and 38 to maintain decoding fidelity.Nucleic acids research · 2020Article
- The Israeli acute paralysis virus IRES captures host ribosomes by mimicking a ribosomal state with hybrid tRNAs.The EMBO journal · 2019Article
- Advances that facilitate the study of large RNA structure and dynamics by nuclear magnetic resonance spectroscopy.Wiley interdisciplinary reviews. RNA · 2019Review
- A tRNA-mimic Strategy to Explore the Role of G34 of tRNAInternational journal of molecular sciences · 2019Article
- Article
- IRES-dependent ribosome repositioning directs translation of a +1 overlapping ORF that enhances viral infection.Nucleic acids research · 2018Article
- Functional Insights into the Adjacent Stem-Loop in Honey Bee Dicistroviruses That Promotes Internal Ribosome Entry Site-Mediated Translation and Viral InfectionJournal of virology · 2018Article
- Topological Structure Determination of RNA Using Small-Angle X-Ray Scattering.Journal of molecular biology · 2017Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The dicistrovirus intergenic region internal ribosome entry site (IRES) adopts a triple-pseudoknotted RNA structure and occupies the core ribosomal E, P, and A sites to directly recruit the ribosome and initiate translation at a non-AUG codon. A subset of dicistrovirus IRESs directs translation in the 0 and +1 frames to produce the viral structural proteins and a +1 overlapping open reading frame called ORFx, respectively. Here we show that specific mutations of two unpaired adenosines located at the core of the three-helical junction of the honey bee dicistrovirus Israeli acute paralysis virus (IAPV) IRES PKI domain can uncouple 0 and +1 frame translation, suggesting that the structure adopts distinct conformations that contribute to 0 or +1 frame translation. Using a reconstituted translation system, we show that ribosomes assembled on mutant IRESs that direct exclusive 0 or +1 frame translation lack reading frame fidelity. Finally, a nuclear magnetic resonance/small-angle X-ray scattering hybrid approach reveals that the PKI domain of the IAPV IRES adopts an RNA structure that resembles a complete tRNA. The tRNA shape-mimicry enables the viral IRES to gain access to the ribosome tRNA-binding sites and form intermolecular contacts with the ribosome that are necessary for initiating IRES translation in a specific reading frame.
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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.