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Updated: May 15, 2026

Using the E1A Minigene Tool to Study mRNA Splicing Changes
Published on: April 22, 2021
Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from
Samir Amrane1, Cameron D Mackereth
1Institut Européen de Chimie et Biologie (IECB), University of Bordeaux, 2 rue Robert Escarpit, 33607, Pessac, France.
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.
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