ArticleBiochemistry2014
Binding affinity and cooperativity control U2B″/snRNA/U2A' RNP formation.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
- Proteome profiling of plant Cajal bodies uncovers kingdom-specific components.Nucleic acids research · 2026Article
- Bioinformatics analysis reveals shared molecular pathways for relationship between ulcerative colitis and primary sclerosing cholangitis.Genomics & informatics · 2025Article
- Phylogeny and conservation of plant U2A/U2A', a core splicing component in U2 spliceosomal complex.Planta · 2021Article
- A prometastatic splicing program regulated by SNRPA1 interactions with structured RNA elements.Science (New York, N.Y.) · 2021Article
- Structural and functional modularity of the U2 snRNP in pre-mRNA splicing.Critical reviews in biochemistry and molecular biology · 2019Review
- Molecular principles underlying dual RNA specificity in the Drosophila SNF protein.Nature communications · 2018Article
- Co-evolution of SNF spliceosomal proteins with their RNA targets in trans-splicing nematodes.Genetica · 2016Article
- Retention and splicing complex (RES) - the importance of cooperativity.RNA biology · 2016Article
- Rapid RNA-ligand interaction analysis through high-information content conformational and stability landscapes.Nature communications · 2015Article
- Positional plasticity in regenerating Amybstoma mexicanum limbs is associated with cell proliferation and pathways of cellular differentiation.BMC developmental biology · 2015Article
- Structures of intermediates during RES complex assembly.Scientific reports · 2015Article
- SEDPHAT--a platform for global ITC analysis and global multi-method analysis of molecular interactions.Methods (San Diego, Calif.) · 2015Review
- Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex.Nature structural & molecular biology · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The U1A and U2B″ proteins are components of the U1 and U2 snRNPs, respectively, where they bind to snRNA stemloops. While localization of U1A and U2B″ to their respective snRNP is a well-known phenomenon, binding of U2B″ to U2 snRNA is typically thought to be accompanied by the U2A' protein. The molecular mechanisms that lead to formation of the RNA/U2B″/U2A' complex and its localization to the U2 snRNP are investigated here, using a combination of in vitro RNA-protein and protein-protein fluorescence and isothermal titration calorimetry binding experiments. We find that U2A' protein binds to U2B″ with nanomolar affinity but binds to U1A with only micromolar affinity. In addition, there is RNA-dependent cooperativity (linkage) between protein-protein and protein-RNA binding. The unique combination of tight binding and cooperativity ensures that the U2A'/U2B″ complex is partitioned only to the U2 snRNP.
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