ArticleThe EMBO journal2016
Pseudouridines in U2 snRNA stimulate the ATPase activity of Prp5 during spliceosome assembly.
Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 80 citations in OpenAlex.
- The impact of psuedouridine modification on human tRNA.Biochemical Society transactions · 2026Review
- A Ψ-Ψ codon-anticodon pairing in nonsense suppression and translational recoding.Nature chemical biology · 2026Article
- Systematic analysis of snRNA genes reveals frequent RNU2-2 variants in dominant and recessive developmental and epileptic encephalopathies.Nature genetics · 2026Article
- Molecular Insights into Widespread Pseudouridine RNA Modifications: Implications for Women's Health and Disease.Biology · 2026Review
- Mechanistic insight into the pseudouridylation of RNA.RNA biology · 2025Review
- RNA modifications in health and disease: from mechanistic insights to therapeutic applications.Precision clinical medicine · 2025Review
- Systematic analysis of snRNA genes reveals frequentmedRxiv : the preprint server for health sciences · 2025Article
- RNA processing/modifying enzymes play key roles in the response to thermospermine in Arabidopsis thaliana.The Plant journal : for cell and molecular biology · 2025Article
- Functions and therapeutic applications of pseudouridylation.Nature reviews. Molecular cell biology · 2025Review
- RNA epigenetic modifications as dynamic biomarkers in cancer: from mechanisms to clinical translation.Biomarker research · 2025Review
- Quantitative Proteomics Identifies Profilin-1 as a Pseudouridine-Binding Protein.Journal of the American Chemical Society · 2025Article
- Epitranscriptomic signatures in blood: emerging biomarkers for diagnosis of diabetes and its complications.Frontiers in cell and developmental biology · 2025Review
- RNA modifications: emerging players in the regulation of reproduction and development.Acta biochimica et biophysica Sinica · 2024Review
- DDX RNA helicases: key players in cellular homeostasis and innate antiviral immunity.Journal of virology · 2024Review
- Molecular targets and strategies in the development of nucleic acid cancer vaccines: from shared to personalized antigens.Journal of biomedical science · 2024Review
- Implications of RNA pseudouridylation for cancer biology and therapeutics: a narrative review.Journal of translational medicine · 2024Review
- Decoding the 'Fifth' Nucleotide: Impact of RNA Pseudouridylation on Gene Expression and Human Disease.Molecular biotechnology · 2024Review
- Critical Cellular Functions and Mechanisms of Action of the RNA Helicase UAP56.Journal of molecular biology · 2024Review
- Epitranscriptomic Regulations in the Heart.Physiological research · 2024Review
- Truncated protein isoforms generate diversity of protein localization and function in yeast.Cell systems · 2024Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Pseudouridine (Ψ) is the most abundant internal modification identified in RNA, and yet little is understood of its effects on downstream reactions. Yeast U2 snRNA contains three conserved Ψs (Ψ35, Ψ42, and Ψ44) in the branch site recognition region (BSRR), which base pairs with the pre-mRNA branch site during splicing. Here, we show that blocks to pseudouridylation at these positions reduce the efficiency of pre-mRNA splicing, leading to growth-deficient phenotypes. Restoration of pseudouridylation at these positions using designer snoRNAs results in near complete rescue of splicing and cell growth. These Ψs interact genetically with Prp5, an RNA-dependent ATPase involved in monitoring the U2 BSRR-branch site base-pairing interaction. Biochemical analysis indicates that Prp5 has reduced affinity for U2 snRNA that lacks Ψ42 and Ψ44 and that Prp5 ATPase activity is reduced when stimulated by U2 lacking Ψ42 or Ψ44 relative to wild type, resulting in inefficient spliceosome assembly. Furthermore, in vivo DMS probing analysis reveals that pseudouridylated U2, compared to U2 lacking Ψ42 and Ψ44, adopts a slightly different structure in the branch site recognition region. Taken together, our results indicate that the Ψs in U2 snRNA contribute to pre-mRNA splicing by directly altering the binding/ATPase activity of Prp5.
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Registered trials
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.