Figure 2.

Scheme of the experimental evidence for the presence of amyloid cores in canonical yeast prions. (A) Amyloid cores from Sup35, Ure2, Swi1 and Mot3 are able to make the transition from the soluble and disordered state to amyloid fibrils with cross-β structure. (B) The Sup35 amyloid core is able to promote (seed) the aggregation of the complete Sup35 PFD in vitro. (C) Introduction of Sup35 amyloid core seeds into yeast is able to induce the aggregation of the endogenous Sup35 protein in vivo and, consequently, the expression of the prionic phenotype.