ArticleNucleic acids research2021
An in vitro reconstituted U1 snRNP allows the study of the disordered regions of the particle and the interactions with proteins and ligands.
Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- The U1 snRNP protein U1C and Helix H of U1 snRNA are critical for small molecule splicing modulator function.Nature communications · 2026Article
- Specific protein-RNA interactions are mostly preserved in biomolecular condensates.Science advances · 2024Article
- Effect of RNA-binding proteins on osteogenic differentiation of bone marrow mesenchymal stem cells.Molecular and cellular biochemistry · 2024Article
- Commitment Complex Splicing Factors in Cancers of the Gastrointestinal Tract-An In Silico Study.Bioinformatics and biology insights · 2024Article
- Molecular basis of RNA-binding and autoregulation by the cancer-associated splicing factor RBM39.Nature communications · 2023Article
- HOG1 Mitogen-Activated Protein Kinase Pathway-Related Autophagy Induced by HJournal of fungi (Basel, Switzerland) · 2023Article
- The alternative splicing of intersectin 1 regulated by PTBP1 promotes human glioma progression.Cell death & disease · 2022Article
- Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Exon-independent recruitment of SRSF1 is mediated by U1 snRNP stem-loop 3.The EMBO journal · 2022Article
- Principles and correction of 5'-splice site selection.RNA biology · 2022Review
- CircIL4R activates the PI3K/AKT signaling pathway via the miR-761/TRIM29/PHLPP1 axis and promotes proliferation and metastasis in colorectal cancer.Molecular cancer · 2021Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
U1 small nuclear ribonucleoparticle (U1 snRNP) plays a central role during RNA processing. Previous structures of U1 snRNP revealed how the ribonucleoparticle is organized and recognizes the pre-mRNA substrate at the exon-intron junction. As with many other ribonucleoparticles involved in RNA metabolism, U1 snRNP contains extensions made of low complexity sequences. Here, we developed a protocol to reconstitute U1 snRNP in vitro using mostly full-length components in order to perform liquid-state NMR spectroscopy. The accuracy of the reconstitution was validated by probing the shape and structure of the particle by SANS and cryo-EM. Using an NMR spectroscopy-based approach, we probed, for the first time, the U1 snRNP tails at atomic detail and our results confirm their high degree of flexibility. We also monitored the labile interaction between the splicing factor PTBP1 and U1 snRNP and validated the U1 snRNA stem loop 4 as a binding site for the splicing regulator on the ribonucleoparticle. Altogether, we developed a method to probe the intrinsically disordered regions of U1 snRNP and map the interactions controlling splicing regulation. This approach could be used to get insights into the molecular mechanisms of alternative splicing and screen for potential RNA therapeutics.
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