Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition

Samir Amrane, Karine Rebora, Ilyass Zniber, Denis Dupuy and Cameron D Mackereth ()
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Samir Amrane: Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
Karine Rebora: Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
Ilyass Zniber: Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
Denis Dupuy: Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
Cameron D Mackereth: Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: Abstract 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.

Date: 2014
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DOI: 10.1038/ncomms5595

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