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Updated: Aug 7, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
Published on: January 8, 2015
Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
M M Patino1, J J Liu, J R Glover
1Howard Hughes Medical Institute and the Department of Molecular Genetics and Cell Biology, University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA.
Abstract:
A cytoplasmically inherited genetic element in yeast, [PSI+], was confirmed to be a prionlike aggregate of the cellular protein Sup35 by differential centrifugation analysis and microscopic localization of a Sup35-green fluorescent protein fusion. Aggregation depended on the intracellular concentration and functional state of the chaperone protein Hsp104 in the same manner as did [PSI+] inheritance. The amino-terminal and carboxy-terminal domains of Sup35 contributed to the unusual behavior of [PSI+]. [PSI+] altered the conformational state of newly synthesized prion proteins, inducing them to aggregate as well, thus fulfilling a major tenet of the prion hypothesis.
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