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Spliceosome Structure and Function
Open accessAbstract
Pre-mRNA splicing is catalyzed by the spliceosome, a multimegadalton ribonucleoprotein (RNP) complex comprised of five snRNPs and numerous proteins. Intricate RNA-RNA and RNP networks, which serve to align the reactive groups of the pre-mRNA for catalysis, are formed and repeatedly rearranged during spliceosome assembly and catalysis. Both the conformation and composition of the spliceosome are highly dynamic, affording the splicing machinery its accuracy and flexibility, and these remarkable dynamics are largely conserved between yeast and metazoans. Because of its dynamic and complex nature, obtaining structural information about the spliceosome represents a major challenge. Electron microscopy has revealed the general morphology of several spliceosomal complexes and their snRNP subunits, and also the spatial arrangement of some of their components. X-ray and NMR studies have provided high resolution structure information about spliceosomal proteins alone or complexed with one or more binding partners. The extensive interplay of RNA and proteins in aligning the pre-mRNA's reactive groups, and the presence of both RNA and protein at the core of the splicing machinery, suggest that the spliceosome is an RNP enzyme. However, elucidation of the precise nature of the spliceosome's active site, awaits the generation of a high-resolution structure of its RNP core.
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“Alternative splicing patterns (BOX 1) are regulated by specialized pre-mRNA binding proteins that alter spliceosome assembly at specific splice sites5–8”
From The neurogenetics of alternative splicing (2016) · cites this paper as [5]
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Metadata
- Authors
- Will, C. L., & Luhrmann, R.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-12-30
- Volume
- 3
- Issue
- 7
- Pages
- a003707-a003707
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3119917
- OpenAlex
- W2148393113
- Cited by
- 1,829
- References
- 163
- Citations by year
- 2026: 89 · 2025: 130 · 2024: 141 · 2023: 135 · 2022: 127 · 2021: 170 · 2020: 142 · 2019: 141 · 2018: 122 · 2017: 111 · 2016: 123 · 2015: 100 · 2014: 91 · 2013: 77 · 2012: 63
- Type
- posted content
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- 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, small nuclear ribonucleoproteins, ribonucleoprotein complexes, spliceosome assembly, RNA-RNA interactions, spliceosome structure, active site, RNA-protein interactions
- MeSH terms
- Humans, Models, Genetic, Models, Molecular, Nucleic Acid Conformation, Protein Processing, Post-Translational, Ribonucleoproteins, RNA Precursors, RNA Splicing, Spliceosomes, Ribonucleoproteins, Small Nuclear, Protein Structure, Tertiary, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Catalytic Domain
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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