ArticleJournal of molecular biology2007
Alternative conformations at the RNA-binding surface of the N-terminal U2AF(65) RNA recognition motif.
Article in Journal of molecular biology, 2007. 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, 21 citations in OpenAlex.
- A Comprehensive Analysis of the Alternative Splicing Co-Factor U2AF65B Gene Family Reveals Its Role in Stress Responses and Root Development.International journal of molecular sciences · 2025Article
- Article
- The biological function and clinical significance of SF3B1 mutations in cancer.Biomarker research · 2020Review
- Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination.Nature communications · 2017Article
- Cancer-Associated Mutations Mapped on High-Resolution Structures of the U2AF2 RNA Recognition Motifs.Biochemistry · 2017Article
- A structural perspective of RNA recognition by intrinsically disordered proteins.Cellular and molecular life sciences : CMLS · 2016Review
- Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.Nucleic acids research · 2014Article
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- Detailed close-ups and the big picture of spliceosomes.Current opinion in structural biology · 2008Review
- Structure of a DNA repair substrate containing an alkyl interstrand cross-link at 1.65 A resolution.Biochemistry · 2007Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The essential pre-mRNA splicing factor, U2 auxiliary factor 65KD (U2AF(65)) recognizes the polypyrimidine tract (Py-tract) consensus sequence of the pre-mRNA using two RNA recognition motifs (RRMs), the most prevalent class of eukaryotic RNA-binding domain. The Py-tracts of higher eukaryotic pre-mRNAs are often interrupted with purines, yet U2AF(65) must identify these degenerate Py-tracts for accurate pre-mRNA splicing. Previously, the structure of a U2AF(65) variant in complex with poly(U) RNA suggested that rearrangement of flexible side-chains or bound water molecules may contribute to degenerate Py-tract recognition by U2AF(65). Here, the X-ray structure of the N-terminal RRM domain of U2AF(65) (RRM1) is described at 1.47 A resolution in the absence of RNA. Notably, RNA-binding by U2AF(65) selectively stabilizes pre-existing alternative conformations of three side-chains located at the RNA interface (Arg150, Lys225, and Arg227). Additionally, a flexible loop connecting the beta2/beta3 strands undergoes a conformational change to interact with the RNA. These pre-existing alternative conformations may contribute to the ability of U2AF(65) to recognize a variety of Py-tract sequences. This rare, high-resolution view of an important member of the RRM class of RNA-binding domains highlights the role of alternative side-chain conformations in RNA recognition.
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