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      SMU-2 and SMU-1, Caenorhabditis elegans homologs of mammalian spliceosome-associated proteins RED and fSAP57, work together to affect splice site choice.

      Molecular and Cellular Biology
      Alternative Splicing, Amino Acid Sequence, Animals, Binding Sites, Blotting, Western, Caenorhabditis elegans, Caenorhabditis elegans Proteins, genetics, physiology, Cell Nucleus, metabolism, Cloning, Molecular, Exons, Genes, Reporter, Green Fluorescent Proteins, Luminescent Proteins, Microscopy, Fluorescence, Models, Genetic, Molecular Sequence Data, Mutation, Nuclear Proteins, Phenotype, Physical Chromosome Mapping, Precipitin Tests, RNA, RNA, Double-Stranded, RNA, Messenger, Reverse Transcriptase Polymerase Chain Reaction, Ribonucleases, Sequence Homology, Amino Acid, Spliceosomes

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          Abstract

          Mutations in the Caenorhabditis elegans gene smu-2 suppress mec-8 and unc-52 mutations. It has been proposed that MEC-8 regulates the alternative splicing of unc-52 transcripts, which encode the core protein of perlecan, a basement membrane proteoglycan. We show that mutation in smu-2 leads to enhanced accumulation of transcripts that skip exon 17, but not exon 18, of unc-52, which explains our finding that smu-2 mutations suppress the uncoordination conferred by nonsense mutations in exon 17, but not in exon 18, of unc-52. We conclude that smu-2 encodes a ubiquitously expressed nuclear protein that is 40% identical to the human RED protein, a component of purified spliceosomes. The effects of smu-2 mutation on both unc-52 pre-mRNA splicing and the suppression of mec-8 and unc-52 mutant phenotypes are indistinguishable from the effects of mutation in smu-1, a gene that encodes a protein that is 62% identical to human spliceosome-associated protein fSAP57. We provide evidence that SMU-2 protects SMU-1 from degradation in vivo. In vitro and in vivo coimmunoprecipitation experiments indicate that SMU-2 and SMU-1 bind to each other. We propose that SMU-2 and SMU-1 function together to regulate splice site choice in the pre-mRNAs of unc-52 and other genes.

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