ArticleRNA (New York, N.Y.)2000
Differential recognition of the polypyrimidine-tract by the general splicing factor U2AF65 and the splicing repressor sex-lethal.
Article in RNA (New York, N.Y.), 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 55 citations in OpenAlex.
- Recurrent Neurodevelopmentally Associated Variants of the Pre-mRNA Splicing Factor U2AF2 Alter RNA Binding Affinities and Interactions.Biochemistry · 2024Article
- Development and validation of AI/ML derived splice-switching oligonucleotides.Molecular systems biology · 2024Article
- Article
- Purifying selection against spurious splicing signals contributes to the base composition evolution of the polypyrimidine tract.Journal of evolutionary biology · 2023Article
- Early Splicing Complexes and Human Disease.International journal of molecular sciences · 2023Review
- Mapping the Constrained Coding Regions in the Human Genome to Their Corresponding Proteins.Journal of molecular biology · 2023Article
- 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
- U2AFEMBO reports · 2019Article
- Drosophila Sister-of-Sex-lethal reinforces a male-specific gene expression pattern by controlling Sex-lethal alternative splicing.Nucleic acids research · 2019Article
- A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates.Journal of visualized experiments : JoVE · 2018Article
- In vitro iCLIP-based modeling uncovers how the splicing factor U2AF2 relies on regulation by cofactors.Genome research · 2018Article
- PolyC-binding proteins enhance expression of the CDK2 cell cycle regulatory protein via alternative splicing.Nucleic acids research · 2018Article
- Promiscuity in post-transcriptional control of gene expression: Drosophila sex-lethal and its regulatory partnerships.FEBS letters · 2017Review
- αCP binding to a cytosine-rich subset of polypyrimidine tracts drives a novel pathway of cassette exon splicing in the mammalian transcriptome.Nucleic acids research · 2016Article
- Diverse regulation of 3' splice site usage.Cellular and molecular life sciences : CMLS · 2015Review
- Differential evolution of signal-responsive RNA elements and upstream factors that control alternative splicing.Cellular and molecular life sciences : CMLS · 2014Review
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- Article
- Control of alternative splicing by forskolin through hnRNP K during neuronal differentiation.Nucleic acids research · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The polypyrimidine-tract (Py-tract) adjacent to 3' splice sites is an essential splicing signal and is recognized by several proteins, including the general splicing factor U2AF65 and the highly specific splicing repressor Sex-lethal (SXL). They both contain ribonucleoprotein-consensus RNA-binding motifs. However, U2AF65 recognizes a wide variety of Py-tracts, whereas SXL recognizes specific Py-tracts such as the nonsex-specific Py-tract of the transformer pre-mRNA. It is not understood how these seemingly similar proteins differentially recognize the Py-tract. To define these interactions, we used chemical interference and protection assays, saturation mutagenesis, and RNAs containing modified nucleotides. We find that these proteins recognize distinct features of the RNA. First, although uracils within the Py-tract are protected from chemical modification by both of these proteins, modification of any one of seven uracils by hydrazine, or any of eight phosphates by ethylnitrosourea strongly interfered with the binding of SXL only. Second, the 2' hydroxyl groups or backbone conformation appeared important for the binding of SXL, but not U2AF65. Third, although any of the bases (cytosine >> adenine > guanine) could substitute for uracils for U2AF65 binding, only guanine partially substituted for certain uracils for SXL binding. The different dependence on individual contacts and nucleotide preference may provide a basis for the different RNA-binding specificities and thus functions of U2AF65 and SXL in 3' splice site choice.
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