ArticleBiochemistry2014
Linkage and allostery in snRNP protein/RNA complexes.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- The mRNA repressor TRIM71 cooperates with Nonsense-Mediated Decay factors to destabilize the mRNA of CDKN1A/p21.Nucleic acids research · 2019Article
- 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
- RNA and Proteins: Mutual Respect.F1000Research · 2017Review
- 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
- Structures of intermediates during RES complex assembly.Scientific reports · 2015Article
- Cooperative structure of the heterotrimeric pre-mRNA retention and splicing complex.Nature structural & molecular biology · 2014Article
- Binding affinity and cooperativity control U2B″/snRNA/U2A' RNP formation.Biochemistry · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Drosophila SNF is a member of the U1A/U2B″/SNF protein family that is found in U1 and U2 snRNPs, where it binds to Stemloop II and Stemloop IV of U1 and U2 snRNA, respectively. SNF also binds to the U2A' protein, but only in the U2 snRNP. Although previous reports have implicated U2A' as a necessary auxiliary protein for the binding of SNF to Stemloop IV, there are no mechanisms that explain the partitioning of U2A' to the U2 snRNP and its absence from the U1 snRNP. Using in vitro RNA binding isotherms and isothermal titration calorimetry, the thermodynamics of SNF/RNA/U2A' ternary complex formation have now been characterized. There is a very large binding cooperativity unique to Stemloop IV that favors formation of the SLIV/SNF/U2A' complex. The binding cooperativity, or heterotropic linkage, is interpreted with respect to linked conformational equilibria of both SNF and its RNA ligand and so represents an example of protein-RNA allostery.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.