Fig. 7

The NURR domain mediates the specific recognition of miR-3470 hEXO-motif. a Binding of the NURR domain to the AGGCU hEXO-motif monitored by NMR. Left: superimposition of the free (black) and RNA-bound (1:1 ratio, red) protein spectra. Right: zoom of the boxed region. Residues names are annotated. b Residues whose amide resonances are affected by the binding of the hEXO RNA are mapped in blue on the surface of the NURR domain. c Residues with significantly perturbed resonances upon hEXO binding are indicated with an asterisk above the sequences of the human and Drosophila proteins. d Binding of the four-domain NeR1R2R3 construct to the AGGCU hEXO-motif. Left: superimposition of the free (black) and RNA-bound (1:1 ratio, orange) protein spectra. Right: zoom of the boxed region. Residues names are annotated as in b. e Binding of the four-domain (NeR1R2R3) protein to wild-type miR-3470 (hEXO) and mutant miR-3470 (ΔhEXO) monitored by BLI. The hEXO and mutated sequences are highlighted in the inset in blue and red, respectively. BLI response values are plotted against the protein concentrations and normalised for better comparison. Dissociation constants are reported. f Binding of the three-domain construct (eR1R2R3) lacking the NURR domain to wild-type and mutant miR-3470, as in e. In the absence of the NURR domain, the protein no longer recognises the cognate RNA