ArticleMolecular and cellular biology1999
Substrate specificities of SR proteins in constitutive splicing are determined by their RNA recognition motifs and composite pre-mRNA exonic elements.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed.
- Molecular characterization of transformer, transformer-2, and doublesex genes in the carambola fruit fly, Bactrocera carambolae, revealing potential for genetic pest management.Insect science · 2026Article
- Towards understandings of serine/arginine-rich splicing factors.Acta pharmaceutica Sinica. B · 2023Review
- Article
- Exon-independent recruitment of SRSF1 is mediated by U1 snRNP stem-loop 3.The EMBO journal · 2022Article
- Review
- The RNA binding protein SRSF1 is a master switch of gene expression and regulation in the immune system.Cytokine & growth factor reviews · 2021Review
- HIV-1: To Splice or Not to Splice, That Is the Question.Viruses · 2021Review
- The transformer-2 and fruitless characterisation with developmental expression profiles of sex-determining genes in Bactrocera dorsalis and B. correcta.Scientific reports · 2020Article
- RNA-Binding Proteins as Important Regulators of Long Non-Coding RNAs in Cancer.International journal of molecular sciences · 2020Review
- Specific inhibition of splicing factor activity by decoy RNA oligonucleotides.Nature communications · 2019Article
- Myelodysplastic Syndrome-Associated SRSF2 Mutations Cause Splicing Changes by Altering Binding Motif Sequences.Frontiers in genetics · 2019Article
- SRSF2 mutations drive oncogenesis by activating a global program of aberrant alternative splicing in hematopoietic cells.Leukemia · 2018Article
- Myelodysplasia-associated mutations in serine/arginine-rich splicing factor SRSF2 lead to alternative splicing of CDC25C.BMC molecular biology · 2016Article
- The Role of Alternative Splicing in the Control of Immune Homeostasis and Cellular Differentiation.International journal of molecular sciences · 2015Review
- Emerging functions of SRSF1, splicing factor and oncoprotein, in RNA metabolism and cancer.Molecular cancer research : MCR · 2014Review
- Article
- Splicing factor SRSF3 is crucial for hepatocyte differentiation and metabolic function.Nature communications · 2013Article
- The RNA-binding landscapes of two SR proteins reveal unique functions and binding to diverse RNA classes.Genome biology · 2012Article
- Son maintains accurate splicing for a subset of human pre-mRNAs.Journal of cell science · 2011Article
- The RNA binding motif protein 15B (RBM15B/OTT3) is a functional competitor of serine-arginine (SR) proteins and antagonizes the positive effect of the CDK11p110-cyclin L2α complex on splicing.The Journal of biological chemistry · 2011Article
13 more citing papers are in PubMed but not listed here.
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5 authors.
Funding
Abstract
We report striking differences in the substrate specificities of two human SR proteins, SF2/ASF and SC35, in constitutive splicing. beta-Globin pre-mRNA (exons 1 and 2) is spliced indiscriminately with either SR protein. Human immunodeficiency virus tat pre-mRNA (exons 2 and 3) and immunoglobulin mu-chain (IgM) pre-mRNA (exons C3 and C4) are preferentially spliced with SF2/ASF and SC35, respectively. Using in vitro splicing with mutated or chimeric derivatives of the tat and IgM pre-mRNAs, we defined specific combinations of segments in the downstream exons, which mediate either positive or negative effects to confer SR protein specificity. A series of recombinant chimeric proteins consisting of domains of SF2/ASF and SC35 in various combinations was used to localize trans-acting domains responsible for substrate specificity. The RS domains of SF2/ASF and SC35 can be exchanged without effect on substrate specificity. The RNA recognition motifs (RRMs) of SF2/ASF are active only in the context of a two-RRM structure, and RRM2 has a dominant role in substrate specificity. In contrast, the single RRM of SC35 can function alone, but its substrate specificity can be influenced by the presence of an additional RRM. The RRMs behave as modules that, when present in different combinations, can have positive, neutral, or negative effects on splicing, depending upon the specific substrate. We conclude that SR protein-specific recognition of specific positive and negative pre-mRNA exonic elements via one or more RRMs is a crucial determinant of the substrate specificity of SR proteins in constitutive splicing.
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