A U1-U2 snRNP interaction network during intron definition
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The assembly of prespliceosomes is responsible for selection of intron sites for splicing. U1 and U2 snRNPs recognize 5' splice sites and branch sites, respectively; although there is information regarding the composition of these complexes, little is known about interaction among the components or between the two snRNPs. Here we describe the protein network of interactions linking U1 and U2 snRNPs with the ATPase Prp5, important for branch site recognition and fidelity during the first steps of the reaction, using fission yeast Schizosaccharomyces pombe. The U1 snRNP core protein U1A binds to a novel SR-like protein, Rsd1, which has homologs implicated in transcription. Rsd1 also contacts S. pombe Prp5 (SpPrp5), mediated by SR-like domains in both proteins. SpPrp5 then contacts U2 snRNP through SF3b, mediated by a conserved DPLD motif in Prp5. We show that mutations in this motif have consequences not only in vitro (defects in prespliceosome formation) but also in vivo, yielding intron retention and exon skipping defects in fission yeast and altered intron recognition in budding yeast Saccharomyces cerevisiae, indicating that the U1-U2 network provides critical, evolutionarily conserved contacts during intron definition.
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Protein levels of Sf3b1 decreased 7-fold during granulopoiesis.
“Protein levels of Sf3b1, for example, which has been recently shown to be essential for intron definition (Shao et al., 2012”
From Orchestrated Intron Retention Regulates Normal Granulocyte Differentiation (2013) · cites this paper as Shao et al., 2012
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- Authors
- Shao, W., Kim, H.-S., Cao, Y., Xu, Y.-Z., & Query, C. C.
- Affiliations
- Chinese Academy of Sciences (CN)
- Albert Einstein College of Medicine (US)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2012-01-01
- Volume
- 32
- Issue
- 2
- Pages
- 470-478
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC3255776
- OpenAlex
- W1965463749
- Cited by
- 85
- References
- 44
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 8 · 2020: 8 · 2019: 8 · 2018: 7 · 2017: 5 · 2016: 5 · 2015: 4 · 2014: 5 · 2013: 9 · 2012: 8
- FWCI
- 2.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Irma T. Hirschl Trust
- National Natural Science Foundation of China (30972622)
- Science and Technology Commission of Shanghai Municipality
- National Institutes of Health
- National Cancer Institute
- National Institute of General Medical Sciences (GM57829, R01GM057829)
- 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 › Nuclear Structure and Function
- Keywords
- U1 snRNP, U2 snRNP, U1A, SF3b, protein-protein interaction network, intron retention, exon skipping, Schizosaccharomyces pombe, Saccharomyces cerevisiae
- MeSH terms
- Adenosine Triphosphatases, Amino Acid Sequence, Introns, Mutation, Phosphoric Monoester Hydrolases, Protein Binding, RNA, Small Nuclear, Saccharomyces cerevisiae, Schizosaccharomyces, Conserved Sequence, Ribonucleoprotein, U2 Small Nuclear, Amino Acid Motifs, Protein Interaction Mapping, Saccharomyces cerevisiae Proteins, Schizosaccharomyces pombe Proteins, Protein Interaction Domains and Motifs
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