PreprintCited by 1,829RNA Research and SplicingRNA and protein synthesis mechanismsRNA regulation and disease

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Spliceosome Structure and Function

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Will, C. L., Luhrmann, R.·2011·Cold Spring Harbor Perspectives in Biology

DOI 10.1101/cshperspect.a003707PMC PMC3119917

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Abstract

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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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)
DOI: 10.1101/cshperspect.a003707
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

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