ArticleNature2017
Structure of a spliceosome remodelled for exon ligation.
Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.
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Who cites it
99 citing papers in PubMed, 184 citations in OpenAlex.
- Human DEAH-box helicase 8 regulates HSF1-mediated stress response and cancer-associated pre-mRNA splicing in tumour cells.NAR cancer · 2026Article
- New mechanistic insights into Prp22-mediated exon ligation and mRNA release.Nucleic acids research · 2025Article
- Brr2p-mediated unwinding of U4/U6 is promoted by a mutually exclusive intra-molecular stem loop in U4 and involves destabilization of the 5' stem-loop of U4.bioRxiv : the preprint server for biology · 2025Article
- Structures of aberrant spliceosome intermediates on their way to disassembly.Nature structural & molecular biology · 2025Article
- The green side of splicing: algal spliceosome shows remarkable structural conservation.The EMBO journal · 2025Article
- Split-APEX implicates splicing factor SRSF1 and splicing helicases in ribosomal biogenesis.Frontiers in molecular biosciences · 2025Article
- Knockout ofBiomedicines · 2024Article
- Characterization of Cwc2, U6 snRNA, and Prp8 interactions destabilized by Prp16 ATPase at the transition between the first and second steps of splicing.RNA (New York, N.Y.) · 2024Article
- Intron lariat spliceosomes convert lariats to true circles: implications for intron transposition.Genes & development · 2024Article
- Intron-lariat spliceosomes convert lariats to true circles: implications for intron transposition.bioRxiv : the preprint server for biology · 2024Article
- An integrative platform for detection of RNA 2'-O-methylation reveals its broad distribution on mRNA.Cell reports methods · 2024Article
- Structural basis of branching during RNA splicing.Nature structural & molecular biology · 2024Article
- Splicing factor Prp18p promotes genome-wide fidelity of consensus 3'-splice sites.Nucleic acids research · 2023Article
- Article
- An ATP-independent role for Prp16 in promoting aberrant splicing.Nucleic acids research · 2023Article
- Biochemical and genetic evidence supports Fyv6 as a second-step splicing factor inRNA (New York, N.Y.) · 2023Article
- Spliceosome assembly and regulation: insights from analysis of highly reduced spliceosomes.RNA (New York, N.Y.) · 2023Review
- Regulation of 3' splice site selection after step 1 of splicing by spliceosomal C* proteins.Science advances · 2023Article
- Biochemical and Genetic Evidence Supports Fyv6 as a Second-Step Splicing Factor inbioRxiv : the preprint server for biology · 2023Article
- Recent advances and current trends in cryo-electron microscopy.Current opinion in structural biology · 2022Review
39 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
The spliceosome excises introns from pre-mRNAs in two sequential transesterifications-branching and exon ligation-catalysed at a single catalytic metal site in U6 small nuclear RNA (snRNA). Recently reported structures of the spliceosomal C complex with the cleaved 5' exon and lariat-3'-exon bound to the catalytic centre revealed that branching-specific factors such as Cwc25 lock the branch helix into position for nucleophilic attack of the branch adenosine at the 5' splice site. Furthermore, the ATPase Prp16 is positioned to bind and translocate the intron downstream of the branch point to destabilize branching-specific factors and release the branch helix from the active site. Here we present, at 3.8 Å resolution, the cryo-electron microscopy structure of a Saccharomyces cerevisiae spliceosome stalled after Prp16-mediated remodelling but before exon ligation. While the U6 snRNA catalytic core remains firmly held in the active site cavity of Prp8 by proteins common to both steps, the branch helix has rotated by 75° compared to the C complex and is stabilized in a new position by Prp17, Cef1 and the reoriented Prp8 RNase H-like domain. This rotation of the branch helix removes the branch adenosine from the catalytic core, creates a space for 3' exon docking, and restructures the pairing of the 5' splice site with the U6 snRNA ACAGAGA region. Slu7 and Prp18, which promote exon ligation, bind together to the Prp8 RNase H-like domain. The ATPase Prp22, bound to Prp8 in place of Prp16, could interact with the 3' exon, suggesting a possible basis for mRNA release after exon ligation. Together with the structure of the C complex, our structure of the C* complex reveals the two major conformations of the spliceosome during the catalytic stages of splicing.
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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.