title: Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from C. elegans.
abstract: The splicing factor SUP-12 from Caenorhabditis elegans binds to regulatory RNA elements in pre-mRNA in order to generate tissue-specific alternative splicing for genes such as the fibroblast growth factor receptor egl-15. In nematode muscle cells, SUP-12 promotes the use of a mutually exclusive exon to impart variant binding specificity to the EGL-15 extracellular protein domain. Here we report the side chain and backbone (1)H, (13)C and (15)N chemical shift assignments for the bacterially expressed RNA recognition motif domain from SUP-12, both in isolation as well as bound to a short RNA derived from the intron sequence between exon 4 and exon 5B of egl-15. Comparison of protein chemical shift values for both the backbone and side chain nuclei, coupled with secondary chemical shift analysis, reveal initial details of the RNA recognition.
authors: Institut Européen de Chimie et Biologie (IECB), University of Bordeaux, 2 rue Robert Escarpit, 33607, Pessac, France.
authors: Samir
authors: S
authors: Amrane
authors: Cameron D
authors: CD
authors: Mackereth
mesh_terms: D017398:Alternative Splicing / Q000235:genetics*; D000818:Animals; D017173:Caenorhabditis elegans / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry*
chemical_list: D029742:Caenorhabditis elegans Proteins; D016601:RNA-Binding Proteins; C525043:Sup-12 protein, C elegans; D012313:RNA