Fig. 9

The three RRM domains of Syncrip participate in and are required for the specific high-affinity interaction between Syncrip and miR-3470. a Binding of the human Syncrip N and NeR1R2R3 proteins to a 14mer miR-3470 RNA (left) and to a full-length miR-3470 (right), monitored by BLI. The BLI response values are plotted against protein concentration, fitted isotherms are shown as continuous lines. b Expanded view of three well dispersed regions of the HSQC spectrum of human Syncrip NeR1R2R3. The free spectrum (black) is superimposed with that of the protein bound to the AGGCU hEXO-motif at 1:1 ratio (orange). Upon addition of the RNA, resonances belonging to the NURR domain RNA-binding surface shift, while resonances of the RRM domains are not perturbed. Peaks are labelled according to the domain the residue locates to. c Expanded view of HSQC spectrum as in b, but employing full-length miR-3470. Upon addition of the RNA, resonances from all four domains are perturbed demonstrating their involvement in binding