ArticleNature structural & molecular biology2016
An accurately preorganized IRES RNA structure enables eIF4G capture for initiation of viral translation.
Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
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Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Structure and function of type IV IRES in picornaviruses: a systematic review.Frontiers in microbiology · 2024Pooled it
- Review
- Article
- An RNA Language Model trained on sequence alone reveals the structural logic of Internal Ribosome Entry Sites.bioRxiv : the preprint server for biology · 2026Article
- The mechanism of ribosomal recruitment during translation initiation on the Type 2 encephalomyocarditis virus IRES.The EMBO journal · 2026Article
- Identification of a novel equine rhinitis B virus detected in horse from Japan.The Journal of veterinary medical science · 2026Article
- Structures of the eIF4G-binding RNA domains among picornaviral IRES types are topologically conserved.Nature communications · 2026Article
- Application of NMR to Large RNAs.Journal of molecular biology · 2025Review
- Review
- Evaluation of synthetic mRNA with selected UTR sequences and alternative poly(A) tail,Molecular therapy. Nucleic acids · 2025Article
- Deep generalizable prediction of RNA secondary structure via base pair motif energy.Nature communications · 2025Article
- Robust genome and cell engineering via in vitro and in situ circularized RNAs.Nature biomedical engineering · 2025Article
- Pyroptosis: Induction and inhibition strategies for immunotherapy of diseases.Acta pharmaceutica Sinica. B · 2024Review
- Translation of Overlapping Open Reading Frames Promoted by Type 2 IRESs in Avian Calicivirus Genomes.Viruses · 2024Article
- Article
- RNA-based translation activators for targeted gene upregulation.Nature communications · 2023Article
- Integrative solution structure of PTBP1-IRES complex reveals strong compaction and ordering with residual conformational flexibility.Nature communications · 2023Article
- The structure and mechanism of action of a distinct class of dicistrovirus intergenic region IRESs.Nucleic acids research · 2023Article
- RNA structure determination: From 2D to 3D.Fundamental research · 2023Review
- Small Molecules Targeting Viral RNA.International journal of molecular sciences · 2023Review
Corrections and comments
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Authors and funding
5 authors.
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Abstract
Many viruses bypass canonical cap-dependent translation in host cells by using internal ribosomal entry sites (IRESs) in their transcripts; IRESs hijack initiation factors for the assembly of initiation complexes. However, it is currently unknown how IRES RNAs recognize initiation factors that have no endogenous RNA binding partners; in a prominent example, the IRES of encephalomyocarditis virus (EMCV) interacts with the HEAT-1 domain of eukaryotic initiation factor 4G (eIF4G). Here we report the solution structure of the J-K region of this IRES and show that its stems are precisely organized to position protein-recognition bulges. This multisite interaction mechanism operates on an all-or-nothing principle in which all domains are required. This preorganization is accomplished by an 'adjuster module': a pentaloop motif that acts as a dual-sided docking station for base-pair receptors. Because subtle changes in the orientation abrogate protein capture, our study highlights how a viral RNA acquires affinity for a target protein.
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