Structural highlights
Publication Abstract from PubMed
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.
Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition.,Amrane S, Rebora K, Zniber I, Dupuy D, Mackereth CD Nat Commun. 2014 Sep 3;5:4595. doi: 10.1038/ncomms5595. PMID:25183497[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Amrane S, Rebora K, Zniber I, Dupuy D, Mackereth CD. Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition. Nat Commun. 2014 Sep 3;5:4595. doi: 10.1038/ncomms5595. PMID:25183497 doi:http://dx.doi.org/10.1038/ncomms5595
