Abstract
MANY proteins involved in pre mRNA processing contain one or more copies of a 70–90-amino-acid αβ module called the ribo-nucleoprotein domain1–4. RNA maturation depends on the specific recognition by ribonucleoproteins of RNA elements within pre-mRNAs and small nuclear RNAs. The human U1A protein binds an RNA hairpin during splicing5–8, and regulates its own expression by binding an internal loop9 in the 3'-untranslated region of its pre-mRNA, preventing polyadenylation. Here we report the nuclear magnetic resonance structure of the complex between the regulatory element of the U1A 3 -untranslated region (UTR)9–11 and the U1A protein RNA-binding domain. Specific intermolecular recognition requires the interaction of the variable loops of the ribonucleoprotein domain with the well-structured helical regions of the RNA. Formation of the complex then orders the flexible RNA single-stranded loop against the protein β-sheet surface, and reorganizes the car-boxy-terminal region of the protein to maximize surface complementarity and functional group recognition.
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Allain, FT., Gubser, C., Howe, P. et al. Specificity of ribonucleoprotein interaction determined by RNA folding during complex formation. Nature 380, 646–650 (1996). https://doi.org/10.1038/380646a0
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DOI: https://doi.org/10.1038/380646a0
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