Fig. 5: Effect of αS domains on the partitioning within TDP-43PrLD – RNA droplets using deletion mutants. | Communications Biology

Fig. 5: Effect of αS domains on the partitioning within TDP-43PrLD – RNA droplets using deletion mutants.

From: α-Synuclein emulsifies TDP-43 prion-like domain—RNA liquid droplets to promote heterotypic amyloid fibrils

Fig. 5

Confocal microscopy images of TDP-43PrLD—RNA preformed droplets immediately upon the addition of αS ΔNTD at 0 hours (a), FRAP data showing the recovery of the αS ΔNTD droplets (b) and TDP-43PrLD droplets. Insets indicate pre-bleach, bleach, and post-bleach images (c). d Fluorescence intensity analysis of the merged images of co-incubated TDP-43PrLD—RNA droplets and αS ΔNTD. Intensity corresponds to the white dotted line across the droplets. e Partitioning of αS ΔNAC in the preformed droplets of TDP-43PrLD—RNA at 0 h. f–h FRAP data showing the recovery of αS ΔNAC (f) and TDP-43PrLD (g) along with intensity analysis of the merged section of the αS ΔNAC-TDP-43PrLD co-incubated reactions. The same reactions at 0-hour were further monitored after 24 h (i–p) to investigate subtle differences in the morphology and internal dynamics of liquid droplets. Scale bar of images = 5 µm, FRAP insets = 2 µm.

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