ArticleThe EMBO journal2006
Proximity of conserved U6 and U2 snRNA elements to the 5' splice site region in activated spliceosomes.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 57 citations in OpenAlex.
- Mutations in the small nuclear RNA gene RNU2-2 cause a severe neurodevelopmental disorder with prominent epilepsy.Nature genetics · 2025Article
- Analysis of R-loop forming regions identifies RNU2-2 and RNU5B-1 as neurodevelopmental disorder genes.Nature genetics · 2025Article
- TDP-43 regulates site-specific 2'-O-methylation of U1 and U2 snRNAs via controlling the Cajal body localization of a subset of C/D scaRNAs.Nucleic acids research · 2019Article
- Postsplicing-Derived Full-Length Intron Circles in the Protozoan ParasiteFrontiers in cellular and infection microbiology · 2018Article
- Life and Death of mRNA Molecules inFrontiers in cellular and infection microbiology · 2018Review
- Dramatically reduced spliceosome in Cyanidioschyzon merolae.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Evolution of group II introns.Mobile DNA · 2015Article
- The organization of RNA contacts by PTB for regulation of FAS splicing.Nucleic acids research · 2014Article
- Post-transcriptional modifications modulate conformational dynamics in human U2-U6 snRNA complex.RNA (New York, N.Y.) · 2014Article
- RNA structure analysis of human spliceosomes reveals a compact 3D arrangement of snRNAs at the catalytic core.The EMBO journal · 2013Article
- Conformational heterogeneity of the protein-free human spliceosomal U2-U6 snRNA complex.RNA (New York, N.Y.) · 2013Article
- Widespread recognition of 5' splice sites by noncanonical base-pairing to U1 snRNA involving bulged nucleotides.Genes & development · 2012Article
- Structure of the yeast U2/U6 snRNA complex.RNA (New York, N.Y.) · 2012Article
- Cwc2 and its human homologue RBM22 promote an active conformation of the spliceosome catalytic centre.The EMBO journal · 2012Article
- Spliceosome structure and function.Cold Spring Harbor perspectives in biology · 2011Review
- Single-molecule analysis of protein-free U2-U6 snRNAs.Nature structural & molecular biology · 2009Article
- Minimum-energy path for a u6 RNA conformational change involving protonation, base-pair rearrangement and base flipping.Journal of molecular biology · 2009Article
- Protein-free small nuclear RNAs catalyze a two-step splicing reaction.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Recognition of atypical 5' splice sites by shifted base-pairing to U1 snRNA.Nature structural & molecular biology · 2009Article
- The use of simple model systems to study spliceosomal catalysis.RNA (New York, N.Y.) · 2009Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Major structural changes occur in the spliceosome during its catalytic activation, which immediately precedes the splicing of pre-mRNA. Whereas changes in snRNA conformation are well documented at the level of secondary RNA-RNA interactions, little is known about the tertiary structure of this RNA-RNA network, which comprises the spliceosome's catalytic core. Here, we have used the hydroxyl-radical probe Fe-BABE, tethered to the tenth nucleotide (U(+10)) of the 5' end of a pre-mRNA intron, to map RNA-RNA proximities in spliceosomes. These studies revealed that several conserved snRNA regions are close to U(+10) in activated spliceosomes, namely (i) the U6 snRNA ACAGAG-box region, (ii) portions of the U6 intramolecular stem-loop (U6-ISL) including a nucleotide implicated in the first catalytic step (U74), and (iii) the region of U2 that interacts with the branch point. These data constrain the relative orientation of these structural elements with respect to U(+10) in the activated spliceosome. Upon conversion of the activated spliceosome to complex C, the accessibility of U6-ISL to hydroxyl-radical cleavage is altered, suggesting rearrangements after the first catalytic step.
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