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

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  • Samir Amrane

    (Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
    Inserm, U869, ARNA Laboratory)

  • Karine Rebora

    (Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
    Inserm, U869, ARNA Laboratory)

  • Ilyass Zniber

    (Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
    Inserm, U869, ARNA Laboratory)

  • Denis Dupuy

    (Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
    Inserm, U869, ARNA Laboratory)

  • Cameron D Mackereth

    (Institut Européen de Chimie et Biologie, IECB, Univ. Bordeaux
    Inserm, U869, ARNA Laboratory)

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.

Suggested Citation

  • Samir Amrane & Karine Rebora & Ilyass Zniber & Denis Dupuy & Cameron D Mackereth, 2014. "Backbone-independent nucleic acid binding by splicing factor SUP-12 reveals key aspects of molecular recognition," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5595
    DOI: 10.1038/ncomms5595
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