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A unique mechanism of snRNP core assembly
Open accessPreprint — published as 10.1038/s41467-025-58461-7 · Paper page
Abstract
The assembly of spliceosomal snRNP cores involves seven Sm proteins (D1/D2/F/E/G/D3/B) forming a ring around each snRNA and typically requires several essential assembly chaperones, particularly the SMN-Gemins complex implicated in spinal muscular atrophy (SMA). Strikingly, in budding yeast, snRNP core assembly only involves Brr1, a nonessential homolog of Gemin2. To unravel this enigma, we systematically investigated snRNP core assembly in budding yeast using biochemical and genetic approaches. We discovered two distinct pathways in budding yeast: chaperone-mediated and direct. The chaperone-mediated pathway involves two proteins, Brr1 and a novel protein, Lot5, but is inefficient. Lot5 binds D1/D2/F/E/G to form a heterohexameric ring (6S). Brr1 binds D1/D2/F/E/G and 6S but cannot displace Lot5 to facilitate assembly. Disruption of both BRR1 and LOT5 genes caused mild growth retardation, but LOT5 overexpression substantially impeded growth. The direct pathway uniquely involves F/E/G as a trimer and a stable D1/D2/F/E/G intermediate complex, explaining the non-essentiality of assembly chaperones. These findings unveil a unique assembly mechanism of snRNP cores, illuminate the evolution of assembly chaperones, and suggest avenues for studying SMA pathophysiology.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 49
- 10.1038/nrm3742 · DOI · Paper page
- Will CL , Luhrmann R. Spliceosome structure and function. Cold Spring Harb Perspect Biol 3, (2011). · DOI · Paper page
- 10.1016/S0092-8674(00)80550-4 · DOI · Paper page
- 10.1016/j.semcdb.2014.04.026 · DOI
- 10.1016/j.cell.2008.09.020 · DOI
- 1996, The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro, EMBO J, 15, 2256, 10.1002/j.1460-2075.1996.tb00579.x · DOI
- 10.1074/jbc.M001441200 · DOI
- 10.1093/hmg/9.5.675 · DOI
- 10.1093/hmg/9.5.663 · DOI
- 2021, Identification and structural analysis of the Schizosaccharomyces pombe SMN complex, Nucleic Acids Res, 49, 7207, 10.1093/nar/gkab158 · DOI
- 10.1128/MCB.01407-13 · DOI
- 2023, Mechanism of assembly of snRNP cores assisted by ICln and the SMN complex in fission yeast, iScience, 26, 107604, 10.1016/j.isci.2023.107604 · DOI
- 10.1074/jbc.275.17.12363 · DOI
- 10.1073/pnas.94.18.9920 · DOI
- 10.1073/pnas.152318699 · DOI
- 10.1016/0092-8674(95)90460-3 · DOI
- 10.1038/nrn2670 · DOI · Paper page
- 10.1016/j.molcel.2012.12.009 · DOI
- 10.1261/rna.940708 · DOI
- 10.1016/j.cell.2011.06.043 · DOI
- 10.1074/jbc.M608528200 · DOI
- 10.1074/jbc.M607505200 · DOI
- 10.1074/jbc.M512243200 · DOI
- 10.1083/jcb.147.6.1181 · DOI
- 10.1083/jcb.148.6.1177 · DOI
- 10.1016/j.molcel.2010.03.014 · DOI
- Martinez-Salas E , Embarc-Buh A , Francisco-Velilla R . Emerging Roles of Gemin5: From snRNPs Assembly to Translation Control. Int J Mol Sci 21, (2020). · DOI
- 2023, PICLN modulates alternative splicing and light/temperature responses in plants, Plant Physiol, 191, 1036, 10.1093/plphys/kiac527 · DOI
- 10.1073/pnas.1504541112 · DOI
- 10.1261/rna.059881.116 · DOI
- 1996, Transcriptional pulse-chase analysis reveals a role for a novel snRNP-associated protein in the manufacture of spliceosomal snRNPs, EMBO J, 15, 4368, 10.1002/j.1460-2075.1996.tb00810.x · DOI
- 10.1126/science.274.5287.546 · DOI
- 10.1038/nature00935 · DOI · Paper page
- 10.1016/j.celrep.2019.05.031 · DOI · Paper page
- 10.1093/nar/gkz1135 · DOI
- 10.1128/MCB.25.24.10989-11004.2005 · DOI
- 10.1126/science.abj8754 · DOI · Paper page
- 10.1006/bbrc.2001.4776 · DOI
- 10.1073/pnas.0802287105 · DOI
- 10.1016/j.molcel.2005.12.011 · DOI
- 10.1016/j.jmb.2009.11.006 · DOI
- 10.1074/jbc.M500541200 · DOI
- 10.1006/jmbi.2001.4624 · DOI
- 10.1016/j.brainres.2018.02.022 · DOI
- Ryan OW , et al. Selection of chromosomal DNA libraries using a multiplex CRISPR system. Elife 3, (2014). · DOI
- 10.1016/S0076-6879(02)50957-5 · DOI
- 10.1016/j.pep.2007.03.018 · DOI
- 10.1093/NAR/GKAB1061 · DOI · Paper page
- 10.1093/bioinformatics/btp033 · DOI
Metadata
- Authors
- Wang, Y., Chen, X., Kong, X., Chen, Y., Xiang, Z., Xiang, Y., Hu, Y., Hou, Y., Zhou, S., Shen, C., Mu, L., Su, D., & Zhang, R.
- Affiliations
- Sichuan University (CN)
- Corresponding author
- Zhang, Rundong
- ORCID
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2024-07-10
- Volume
- 16
- Issue
- 1
- Pages
- 3166-3166
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC11965559
- OpenAlex
- W4409148881
- Cited by
- 7
- References
- 1
- Citations by year
- 2026: 4 · 2025: 3
- FWCI
- 2.09
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Nature Communications (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Ministry of Science and Technology of the People's Republic of China (2017YFA0504300, 2017YFA0505900)
- Department of Science and Technology of Sichuan Province (2020YJ0209)
- 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
- Sm proteins, SMN complex, spinal muscular atrophy, spliceosome, Saccharomyces cerevisiae, assembly intermediates
- MeSH terms
- Protein Binding, RNA, Small Nuclear, Saccharomyces cerevisiae, Spliceosomes, Molecular Chaperones, Saccharomyces cerevisiae Proteins, snRNP Core Proteins, SMN Complex Proteins
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