Fig. 5: PolyU promotes hnRNPA1A amyloid formation in the absence of condensation. | Nature Chemistry

Fig. 5: PolyU promotes hnRNPA1A amyloid formation in the absence of condensation.

From: RNA modulates hnRNPA1A amyloid formation mediated by biomolecular condensates

Fig. 5

a, Re-scan confocal fluorescence microscopy images of hnRNPA1A fibrils after 48 h of incubation with 500 ng μl–1 polyU. This condition was taken as representative of the third regime in Fig. 3. Imaging of fibrils with re-scan microscopy in the third regime was repeated with at least two distinct protein preparations. b, TEM image of hnRNPA1A amyloid fibrils in the third regime after 48 h. TEM analysis was conducted on at least two distinct protein preparations. c, ThT aggregation profiles of hnRNPA1A with 500 mM NaCl (in the absence of protein condensation) in the absence (–) and presence (+) of 500 ng μl–1 polyU. The dashed vertical lines show the half-times (t1/2). The aggregation assays were performed in technical triplicates and with two distinct protein preparations.

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