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Cited by 14RNA Research and SplicingRNA and protein synthesis mechanismsRNA regulation and disease

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Structures of aberrant spliceosome intermediates on their way to disassembly

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Soni, Komal, Horvath, Attila, Dybkov, Olexandr, Schwan, Merlin, Trakansuebkul, Sasanan, Flemming, Dirk, Wild, Klemens, Urlaub, Henning, Fischer, Tamás, Sinning, Irmgard·2025·Nature Structural & Molecular Biology
DOI 10.1038/s41594-024-01480-7PMC PMC12086092

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Abstract

Abstract Intron removal during pre-mRNA splicing is of extraordinary complexity and its disruption causes a vast number of genetic diseases in humans 1 . While key steps of the canonical spliceosome cycle have been revealed by combined structure-function analyses 2,3 , structural information on an aberrant spliceosome committed to premature disassembly is not available. Here, we report two cryo-EM structures of post-B act spliceosome intermediates from S. pombe primed for disassembly. We identify the DEAH-box helicase – G patch protein pair (Gih35-Gpl1, homologous to human DHX35-GPATCH1) and show how it maintains catalytic dormancy. In both structures, Gpl1 recognizes a remodeled active site introduced by an over-stabilization of the U5 loop I interaction with the 5’ exon leading to a single nucleotide insertion at the 5’splice site. Remodeling is communicated to the spliceosome surface and the Ntr1 complex that mediates disassembly is recruited. Our data pave the way for a targeted analysis of splicing quality control.

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Metadata

Authors
Soni, K., Horvath, A., Dybkov, O., Schwan, M., Trakansuebkul, S., Flemming, D., Wild, K., Urlaub, H., Fischer, T., & Sinning, I.
Affiliations
  • Heidelberg University (DE)
  • Max Planck Institute for Multidisciplinary Sciences (DE)
  • Australian National University (AU)
  • Universitätsmedizin Göttingen (DE)
Corresponding author
  • Soni, Komal
  • Fischer, Tamás
  • Sinning, Irmgard
ORCID
Venue
Nature Structural & Molecular Biology
Publisher
Springer Science and Business Media LLC
Published
2025-01-20
Volume
32
Issue
5
Pages
914-925
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
DOI
10.1038/s41594-024-01480-7
PMC
PMC12086092
OpenAlex
W4406633361
Cited by
14
References
4
Citations by year
2026: 7 · 2025: 7
FWCI
4.21
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Structural & Molecular Biology (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • GoeScholar The Publication Server of the Georg-August-Universität Göttingen (Georg-August-Universität Göttingen) (submittedVersion, cc-by-nc-nd)
Funders
  • European Molecular Biology Laboratory
  • Deutsche Forschungsgemeinschaft (35/1597‐1, INST 35/1597-1, INST 35/1314-1 FUGG., INST35/1503‐1FUGG, TRR319, INST35/1597‐1FUGG, INST 35/1314‐1, SI 586/6-1, 35/1597-1 FUGG, 35/1503-1, 35/1503-1 FUGG, 439669440, 35/1314-1 FUGG, TP-B03, INST 35/1503‐1, 35/1314-1)
  • Australian Research Council (DP190100423, DP240102611)
  • Leibniz-Gemeinschaft
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
Keywords
spliceosome, pre-mRNA splicing, spliceosome disassembly, DEAH-box helicase, 5' splice site, Schizosaccharomyces pombe, cryo-EM structure
MeSH terms
Humans, Introns, Models, Molecular, RNA Precursors, RNA Splicing, Schizosaccharomyces, Spliceosomes, Catalytic Domain, Cryoelectron Microscopy, Schizosaccharomyces pombe Proteins, DEAD-box RNA Helicases

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