ArticleRNA (New York, N.Y.)2003
Sex lethal and U2 small nuclear ribonucleoprotein auxiliary factor (U2AF65) recognize polypyrimidine tracts using multiple modes of binding.
Article in RNA (New York, N.Y.), 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 49 citations in OpenAlex.
- Reliability and accuracy of single-molecule FRET studies for characterization of structural dynamics and distances in proteins.Nature methods · 2023Article
- MicroSalmon: A Comprehensive, Searchable Resource of Predicted MicroRNA Targets and 3'UTR Cis-Regulatory Elements in the Full-Length Sequenced Atlantic Salmon Transcriptome.Non-coding RNA · 2021Article
- SPF45/RBM17-dependent, but not U2AF-dependent, splicing in a distinct subset of human short introns.Nature communications · 2021Article
- Genomic and cDNA selection-amplification identifies transcriptome-wide binding sites for the Drosophila protein sex-lethal.PloS one · 2021Article
- Regulation of gene expression in trypanosomatids: living with polycistronic transcription.Open biology · 2019Article
- Recognition of the 3' splice site RNA by the U2AF heterodimer involves a dynamic population shift.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions.Frontiers in molecular biosciences · 2016Review
- Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing.RNA (New York, N.Y.) · 2015Article
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- Article
- Analysis of in situ pre-mRNA targets of human splicing factor SF1 reveals a function in alternative splicing.Nucleic acids research · 2011Article
- RNA induces conformational changes in the SF1/U2AF65 splicing factor complex.Journal of molecular biology · 2011Article
- Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1.Journal of molecular biology · 2010Article
- Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65.The Journal of biological chemistry · 2008Article
- Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65.Molecular biology of the cell · 2008Article
- Large-scale comparative analysis of splicing signals and their corresponding splicing factors in eukaryotes.Genome research · 2008Article
- A conditional role of U2AF in splicing of introns with unconventional polypyrimidine tracts.Molecular and cellular biology · 2007Article
- Alternative conformations at the RNA-binding surface of the N-terminal U2AF(65) RNA recognition motif.Journal of molecular biology · 2007Article
- The polypyrimidine tract binding protein (PTB) represses splicing of exon 6B from the beta-tropomyosin pre-mRNA by directly interfering with the binding of the U2AF65 subunit.Molecular and cellular biology · 2006Article
- Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.Molecular cell · 2006Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The molecular basis for specific recognition of simple homopolymeric sequences like the polypyrimidine tract (Py tract) by multiple RNA recognition motifs (RRMs) is not well understood. The Drosophila splicing repressor Sex lethal (SXL), which has two RRMs, can directly compete with the essential splicing factor U2AF(65), which has three RRMs, for binding to specific Py tracts. We have combined site-specific photocross-linking and chemical cleavage of the proteins to biochemically map cross-linking of each of the uracils within the Py tract to specific RRMs. For both proteins, RRM1 and RRM2 together constitute the minimal Py-tract recognition domain. The RRM3 of U2AF(65) shows no cross-linking to the Py tract. Both RRM1 and RRM2 of U2AF(65) and SXL can be cross-linked to certain residues, with RRM2 showing a surprisingly high number of residues cross-linked. The cross-linking data eliminate the possibility that shorter Py tracts are bound by fewer RRMs. We present a model to explain how the binding affinity can nonetheless change as a function of the length of the Py tract. The results indicate that multiple modes of binding result in an ensemble of RNA-protein complexes, which could allow tuning of the binding affinity without changing sequence specificity.
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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.