ArticleRNA (New York, N.Y.)2004
The conserved RNA recognition motif 3 of U2 snRNA auxiliary factor (U2AF 65) is essential in vivo but dispensable for activity in vitro.
Article in RNA (New York, N.Y.), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- UHMK1 aids colorectal cancer cell proliferation and chemoresistance through augmenting IL-6/STAT3 signaling.Cell death & disease · 2022Article
- Evolution of the Early Spliceosomal Complex-From Constitutive to Regulated Splicing.International journal of molecular sciences · 2021Review
- Genomic and cDNA selection-amplification identifies transcriptome-wide binding sites for the Drosophila protein sex-lethal.PloS one · 2021Article
- Architecture and Distribution of Introns in Core Genes of FourG3 (Bethesda, Md.) · 2017Article
- 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
- U2AF65 adapts to diverse pre-mRNA splice sites through conformational selection of specific and promiscuous RNA recognition motifs.Nucleic acids research · 2013Article
- Article
- Genomic mRNA profiling reveals compensatory mechanisms for the requirement of the essential splicing factor U2AF.Molecular and cellular biology · 2011Article
- Comparative analysis of information contents relevant to recognition of introns in many species.BMC genomics · 2011Article
- Solution conformation and thermodynamic characteristics of RNA binding by the splicing factor U2AF65.The Journal of biological chemistry · 2008Article
- Identification of motifs that function in the splicing of non-canonical introns.Genome biology · 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
- Structural basis for polypyrimidine tract recognition by the essential pre-mRNA splicing factor U2AF65.Molecular cell · 2006Article
- Crystallization and preliminary X-ray analysis of a U2AF65 variant in complex with a polypyrimidine-tract analogue by use of protein engineering.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Multiple U2AF65 binding sites within SF3b155: thermodynamic and spectroscopic characterization of protein-protein interactions among pre-mRNA splicing factors.Journal of molecular biology · 2006Article
- Major phosphorylation of SF1 on adjacent Ser-Pro motifs enhances interaction with U2AF65.The FEBS journal · 2006Article
- FRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35.RNA (New York, N.Y.) · 2005Article
- Analysis of mutant phenotypes and splicing defects demonstrates functional collaboration between the large and small subunits of the essential splicing factor U2AF in vivo.Molecular biology of the cell · 2005Article
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6 authors.
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Abstract
The general splicing factor U2AF(65) recognizes the polypyrimidine tract (Py tract) that precedes 3' splice sites and has three RNA recognition motifs (RRMs). The C-terminal RRM (RRM3), which is highly conserved, has been proposed to contribute to Py-tract binding and establish protein-protein contacts with splicing factors mBBP/SF1 and SAP155. Unexpectedly, we find that the human RRM3 domain is dispensable for U2AF(65) activity in vitro. However, it has an essential function in Schizosaccharomyces pombe distinct from binding to the Py tract or to mBBP/SF1 and SAP155. First, deletion of RRM3 from the human protein has no effect on Py-tract binding. Second, RRM123 and RRM12 select similar sequences from a random pool of RNA. Third, deletion of RRM3 has no effect on the splicing activity of U2AF(65) in vitro. However, deletion of the RRM3 domain of S. pombe U2AF(59) abolishes U2AF function in vivo. In addition, certain amino acid substitutions on the four-stranded beta-sheet surface of RRM3 compromise U2AF function in vivo without affecting binding to mBBP/SF1 or SAP155 in vitro. We propose that RRM3 has an unrecognized function that is possibly relevant for the splicing of only a subset of cellular introns. We discuss the implications of these observations on previous models of U2AF function.
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