Fig. 2: Absence of prolines in a perfectly repetitive GLFG variant favors amyloid-like structures.
From: Recapitulation of selective nuclear import and export with a perfectly repeated 12mer GLFG peptide
a Comparison of two perfectly repetitive FG domains. The “Pro-free_prf.GLFG52x12” is a proline-free variant (see also Supplementary Table 1). b Phase-contrast images of FG phases assembled from Mac98A FG domain, the proline-containing prf.GLFG52x12[+GLEBS] and the Pro-free_prf.GLFG52x12. Note that the former two formed spherical particles, but the Pro-free variant formed irregular shapes. The experiment was repeated independently four times with similar results, and representative images are shown. c FG phases were assembled from the indicated FG domains and challenged with Alexa488-labeled NTF2, mCherry, and Thioflavin-T (ThT). Numbers refer to the ratios of fluorescence inside the FG phases to that in the surrounding buffer. Images were taken at 30 min after FG phase assembly. Note that the bright ThT stain of the Pro-free variant is diagnostic of amyloid structures. The N/Q-rich Nup116 FG repeats served as a ThT positive control. See also Supplementary Figs. 1 and 2.
