ArticleNucleic acids research2020
A unique internal ribosome entry site representing a dynamic equilibrium state of RNA tertiary structure in the 5'-UTR of Wheat yellow mosaic virus RNA1.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Conserved Arginine of the Potyviridae Viral Genome-Linked Proteins (VPg) as a Key Determinant for eIF4E Binding.International journal of molecular sciences · 2026Article
- Long-distance RNA-RNA interactions shape dynamic RNA architectures and functional states in plant positive-strand RNA viruses.Frontiers in microbiology · 2026Review
- Conserved Structure Associated with Different 3'CITEs Is Important for Translation of Umbraviruses.Viruses · 2023Article
- Article
- Conserved RNA secondary structure in Cherry virus A 5'-UTR associated with translation regulation.Virology journal · 2022Article
- Translation of Plant RNA Viruses.Viruses · 2021Review
- Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Internal ribosome entry sites (IRESes) were first reported in RNA viruses and subsequently identified in cellular mRNAs. In this study, IRES activity of the 5'-UTR in Wheat yellow mosaic virus (WYMV) RNA1 was identified, and the 3'-UTR synergistically enhanced this IRES activity via long-distance RNA-RNA interaction between C80U81and A7574G7575. Within the 5'-UTR, the hairpin 1(H1), flexible hairpin 2 (H2) and linker region (LR1) between H1 and H2 played an essential role in cap-independent translation, which is associated with the structural stability of H1, length of discontinuous stems and nucleotide specificity of the H2 upper loop and the long-distance RNA-RNA interaction sites in LR1. The H2 upper loop is a target region of the eIF4E. Cytosines (C55, C66, C105 and C108) in H1 and H2 and guanines (G73, G79 and G85) in LR1 form discontinuous and alternative base pairing to maintain the dynamic equilibrium state, which is used to elaborately regulate translation at a suitable level. The WYMV RNA1 5'-UTR contains a novel IRES, which is different from reported IRESes because of the dynamic equilibrium state. It is also suggested that robustness not at the maximum level of translation is the selection target during evolution of WYMV RNA1.
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