ArticleRNA (New York, N.Y.)2004
Modified nucleotides at the 5' end of human U2 snRNA are required for spliceosomal E-complex formation.
Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
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Who cites it
105 citing papers in PubMed, 154 citations in OpenAlex.
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- A magic methyl effect in the active site of a methyltransferase ribozyme.Nature communications · 2026Article
- U2 snRNP recognizes the branch site through a loaded-spring strand-invasion mechanism.Nucleic acids research · 2026Article
- Cap-adjacent 2'-O-ribose methylation of RNA in C. elegans is required for postembryonic growth and germline development in the presence of the decapping exonuclease EOL-1.Nucleic acids research · 2026Article
- The tumour suppressor RBM5 activates the helicase DHX15 to regulate splicing.Research square · 2026Article
- Systematic analysis of snRNA genes reveals frequent RNU2-2 variants in dominant and recessive developmental and epileptic encephalopathies.Nature genetics · 2026Article
- The tumour suppressor RBM5 activates the helicase DHX15 to regulate splicing.bioRxiv : the preprint server for biology · 2026Article
- The human branchpoint-interacting stem-loop sequence and structure regulates U2 snRNA expression, branchpoint recognition, and the transcriptome.Nucleic acids research · 2026Article
- Critical structural perturbations of ribozyme active sites induced by 2'-O-methylation commonly used in structural studies.Nucleic acids research · 2026Article
- Computational limitations and future needs to unravel the full potential of 2'-O-methylation and C/D box snoRNAs.RNA biology · 2025Review
- Mutation of CMTR2 in Lung Adenocarcinoma Alters RNA Alternative Splicing and Reveals Therapeutic Vulnerabilities.Nature communications · 2025Article
- The human branchpoint-interacting stem loop sequence and structure regulates U2 snRNA expression, branchpoint recognition, and transcriptome.bioRxiv : the preprint server for biology · 2025Article
- Review
- Systematic analysis of snRNA genes reveals frequentmedRxiv : the preprint server for health sciences · 2025Article
- Pseudouridine synthases are proviral factors for Sindbis virus in insect and mammalian cells.mBio · 2025Article
- A guide to the biogenesis and functions of endogenous small non-coding RNAs in animals.Nature reviews. Molecular cell biology · 2025Review
- Decoding meLife · 2025Article
- Mapping snoRNA-target RNA interactions in an RNA-binding protein-dependent manner with chimeric eCLIP.Genome biology · 2025Article
- Decoding mbioRxiv : the preprint server for biology · 2025Article
- Mapping snoRNA-target RNA interactions in an RNA binding protein-dependent manner with chimeric eCLIP.bioRxiv : the preprint server for biology · 2024Article
45 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
U2 snRNA, a key player in nuclear pre-mRNA splicing, contains a 5'-terminal m3G cap and many internal modifications. The latter were shown in vertebrates to be generally required for U2 function in splicing, but precisely which residues are essential and their role in snRNP and/or spliceosome assembly is presently not clear. Here, we investigated the roles of individual modified nucleotides of HeLa U2 snRNA in pre-mRNA splicing, using a two-step in vitro reconstitution/complementation assay. We show that the three pseudouridines and five 2'O-methyl groups within the first 20 nucleotides of U2 snRNA, but not the m3G cap, are required for efficient pre-mRNA splicing. Individual pseudouridines were not essential, but had cumulative effects on U2 function. In contrast, four of five 2'O-methylations (at positions 1, 2, 12, and 19) were individually required for splicing. The in vitro assembly of 17S U2 snRNPs was not dependent on the presence of modified U2 residues. However, individual internal modifications were required for the formation of the ATP-independent early spliceosomal E complex. Our data strongly suggest that modifications within the first 20 nucleotides of U2 play an important role in facilitating the interaction of U2 with U1 snRNP and/or other factors within the E complex.
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