ArticleNucleic acids research2007
Eukaryotic ribosomal protein RPS25 interacts with the conserved loop region in a dicistroviral intergenic internal ribosome entry site.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 69 citations in OpenAlex.
- Specialized ribosomes: integrating new insights and current challenges.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- The structure and mechanism of action of a distinct class of dicistrovirus intergenic region IRESs.Nucleic acids research · 2023Article
- Translation dysregulation in neurodegenerative diseases: a focus on ALS.Molecular neurodegeneration · 2023Review
- Initiation of translation on nedicistrovirus and related intergenic region IRESs by their factor-independent binding to the P site of 80S ribosomes.RNA (New York, N.Y.) · 2023Article
- Partners in crime: Proteins implicated in RNA repeat expansion diseases.Wiley interdisciplinary reviews. RNA · 2022Review
- Fatal attraction: The roles of ribosomal proteins in the viral life cycle.Wiley interdisciplinary reviews. RNA · 2021Review
- A memory of eS25 loss drives resistance phenotypes.Nucleic acids research · 2020Article
- Proteomic and mechanistic dissection of the poxvirus-customized ribosome.Journal of cell science · 2020Article
- Ribosome heterogeneity in stem cells and development.The Journal of cell biology · 2020Review
- Article
- Translation from the Ribosome to the Clinic: Implication in Neurological Disorders and New Perspectives from Recent Advances.Biomolecules · 2019Review
- Review
- Small and Large Ribosomal Subunit Deficiencies Lead to Distinct Gene Expression Signatures that Reflect Cellular Growth Rate.Molecular cell · 2019Article
- Heterogeneity and specialized functions of translation machinery: from genes to organisms.Nature reviews. Genetics · 2018Review
- 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
- Hijacking of the AP-1 Signaling Pathway during Development of ATL.Frontiers in microbiology · 2017Review
- Control of tissue size and development by a regulatory element in theAmerican journal of cancer research · 2017Article
- Molecular analysis of the factorless internal ribosome entry site in Cricket Paralysis virus infection.Scientific reports · 2016Article
- Ribosomal proteins: functions beyond the ribosome.Journal of molecular cell biology · 2015Review
- Molecular biology: signals across domains of life.Nature · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intergenic region-internal ribosome entry site (IGR-IRES) of dicistroviruses binds to 40S ribosomal subunits in the absence of eukaryotic initiation factors (eIFs). Although the conserved loop sequences in dicistroviral IGR-IRES elements are protected from chemical modifications in the presence of the 40S subunit, molecular components in the 40S subunit, which interacts with the loop sequences in the IRES, have not been identified. Here, a chemical crosslinking study using 4-thiouridine-labeled IGR-IRES revealed interactions of the IGR-IRES with several 40S proteins but not with the 18S rRNA. The strongest crosslinking signal was identified for ribosomal protein S25 (rpS25). rpS25 is known to be a neighbor of rpS5, which has been shown to interact with a related IGR-IRES by cryo-electron microscopy. Crosslinking analysis with site-directed mutants showed that nucleotides UU(6089-6090), which are located in the loop region in conserved domain 2b in the IRES, appear to interact with rpS25. rpS25 is specific to eukaryotes, which explains why there is no recognition of the IGR-IRES by prokaryotic ribosomes. Although the idea that the IGR-IRES element may be a relict of a primitive translation system has been postulated, our experimental data suggest that the IRES has adapted to eukaryotic ribosomal proteins.
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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.