Nature communications, 2014-09, Vol.5 (1), p.4595-4595, Article 4595
2014
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- Autor(en) / Beteiligte
- Titel
- Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition
- Ist Teil von
- Nature communications, 2014-09, Vol.5 (1), p.4595-4595, Article 4595
- Ort / Verlag
- London: Nature Publishing Group UK
- Erscheinungsjahr
- 2014
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Cellular differentiation is frequently accompanied by alternative splicing, enabled by the expression of tissue-specific factors which bind to pre-mRNAs and regulate exon choice. During Caenorhabditis elegans development, muscle-specific expression of the splicing factor SUP-12, together with a member of the Fox-1 family of splicing proteins, generates a functionally distinct isoform of the fibroblast growth factor receptor EGL-15. Using a combination of NMR spectroscopy and isothermal titration calorimetry, we determined the mode of nucleic acid binding by the RNA recognition motif domain of SUP-12. The calculated structures provide the first atomic details of RNA and DNA binding by the family of proteins that include SUP-12, RBM24, RBM38/RNPC1, SEB-4 and XSeb4R. This information was further used to design strategic mutations to probe the interaction with ASD-1 and to quantitatively perturb splicing in vivo . Alternative splicing is a widespread mechanism used in the control of gene expression during development. Here, Amrane et al. provide molecular level insights into how the RRM-domain muscle-specific factor SUP-12 interacts with its nucleic acid substrates to direct splicing patterns.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 2041-1723eISSN: 2041-1723DOI: 10.1038/ncomms5595Titel-ID: cdi_proquest_miscellaneous_1560094804
- Format
- –
- Schlagworte
- 101/6, 140/131, 38/35, 631/136, 631/337, 64/11, 82/16, 82/80, 82/83, Alternative Splicing, Amino Acid Sequence, Animals, Base Sequence, Caenorhabditis elegans - genetics, Caenorhabditis elegans - growth & development, Caenorhabditis elegans - metabolism, Caenorhabditis elegans Proteins - chemistry, Caenorhabditis elegans Proteins - genetics, Caenorhabditis elegans Proteins - metabolism, Calorimetry, Cell Differentiation, Crystallography, X-Ray, Escherichia coli - genetics, Escherichia coli - metabolism, Gene Expression, Humanities and Social Sciences, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, multidisciplinary, Protein Binding, Receptors, Fibroblast Growth Factor - chemistry, Receptors, Fibroblast Growth Factor - genetics, Receptors, Fibroblast Growth Factor - metabolism, Recombinant Proteins, RNA - chemistry, RNA - metabolism, RNA-Binding Proteins - chemistry, RNA-Binding Proteins - genetics, RNA-Binding Proteins - metabolism, Science, Science (multidisciplinary)