ArticleThe Journal of biological chemistry2008
Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 33 citations in OpenAlex.
- Recurrent Neurodevelopmentally Associated Variants of the Pre-mRNA Splicing Factor U2AF2 Alter RNA Binding Affinities and Interactions.Biochemistry · 2024Article
- Pre-mRNA splicing factor U2AF2 recognizes distinct conformations of nucleotide variants at the center of the pre-mRNA splice site signal.Nucleic acids research · 2022Article
- Representative cancer-associated U2AF2 mutations alter RNA interactions and splicing.The Journal of biological chemistry · 2020Article
- A splice site-sensing conformational switch in U2AF2 is modulated by U2AF1 and its recurrent myelodysplasia-associated mutation.Nucleic acids research · 2020Article
- Article
- SF1 Phosphorylation Enhances Specific Binding to U2AFBiophysical journal · 2016Article
- An extended U2AF(65)-RNA-binding domain recognizes the 3' splice site signal.Nature communications · 2016Article
- Article
- Uniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Structure-guided U2AF65 variant improves recognition and splicing of a defective pre-mRNA.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- A Broad range of conformations contribute to the solution ensemble of the essential splicing factor U2AF(65).Biochemistry · 2012Article
- Three RNA recognition motifs participate in RNA recognition and structural organization by the pro-apoptotic factor TIA-1.Journal of molecular biology · 2012Article
- The 3' splice site of influenza A segment 7 mRNA can exist in two conformations: a pseudoknot and a hairpin.PloS one · 2012Article
- Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq.Nucleic acids research · 2011Article
- Large favorable enthalpy changes drive specific RNA recognition by RNA recognition motif proteins.Biochemistry · 2011Article
- RNA induces conformational changes in the SF1/U2AF65 splicing factor complex.Journal of molecular biology · 2011Article
- Genomic mRNA profiling reveals compensatory mechanisms for the requirement of the essential splicing factor U2AF.Molecular and cellular biology · 2011Article
- Interactions between PTB RRMs induce slow motions and increase RNA binding affinity.Journal of molecular biology · 2010Article
- Interactome for auxiliary splicing factor U2AF(65) suggests diverse roles.Biochimica et biophysica actaArticle
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The U2 auxiliary factor large subunit (U2AF65) is an essential pre-mRNA splicing factor for the initial stages of spliceosome assembly. Tandem RNA recognition motifs (RRM)s of U2AF65 recognize polypyrimidine tract signals adjacent to 3' splice sites. Despite the central importance of U2AF65 for splice site recognition, the relative arrangement of the U2AF65 RRMs and the energetic forces driving polypyrimidine tract recognition remain unknown. Here, the solution conformation of the U2AF65 RNA binding domain determined using small angle x-ray scattering reveals a bilobal shape without apparent interdomain contacts. The proximity of the N and C termini within the inter-RRM configuration is sufficient to explain the action of U2AF65 on spliceosome components located both 5' and 3' to its binding site. Isothermal titration calorimetry further demonstrates that an unusually large enthalpy-entropy compensation underlies U2AF65 recognition of an optimal polyuridine tract. Qualitative similarities were observed between the pairwise distance distribution functions of the U2AF65 RNA binding domain and those either previously observed for N-terminal RRMs of Py tract-binding protein that lack interdomain contacts or calculated from the high resolution coordinates of a U2AF65 deletion variant bound to RNA. To further test this model, the shapes and RNA interactions of the wild-type U2AF65 RNA binding domain were compared with those of U2AF65 variants containing either Py tract-binding protein linker sequences or a deletion within the inter-RRM linker. Results of these studies suggest inter-RRM conformational plasticity as a possible means for U2AF65 to universally identify diverse pre-mRNA splice sites.
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