Figure 1
From: RNA recognition motifs of disease-linked RNA-binding proteins contribute to amyloid formation
Most disease-linked RNA recognition motifs (RRMs) exhibit reversible thermal unfolding and refolding. (A) Domain organization of six RNA-binding proteins shows the ten RRMs (outlined in red box with residue numbers marked at the bottom) used in this study. (B) Overall tertiary structural changes for five RRMs from disease-linked RNA-binding proteins (TDP-43 RRM1, TDP-43 RRM2, FUS RRM, RBM45 RRM1, RBM45 RRM2), and five RRMs from non-disease-associated proteins (U2AF47 RRM1, UP1 RRM1, UP1 RRM2, PABP RRM2, PABP RRM4), assessed by circular dichroism in the near-UV range (260 to 310 nm) during the thermal unfolding and refolding process. We raised the temperature from 20 °C to 90 °C at intervals of 10 °C (marked by different colors, as shown at the bottom of the figure) to induce protein unfolding, and then re-cooled to 20 °C for protein refolding (marked by lines of black asterisks, labeled as “Re-cooled 20 °C”). Each RRM was purified to a high homogeneity, as shown by the SDS-PAGE gels at right of the CD spectra (The full-length gels are shown in the Supplementary Fig. S1).
