Michele L Kadnar

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The types of [PIN+] prions and liquid-like aggregates formed by the yeast protein Rnq1 are controlled by interactions between its non-prion and prion domains

Jan 19, 2025 | biorxiv.org | Irina L. Derkatch |Susan W. Liebman |Monica Andrade |Mónica Andrade |Michele L Kadnar

AbstractPrions are self-propagating protein conformations usually existing as amyloid aggregates. [PIN+], a prion form of the Rnq1 protein frequently found in wild and laboratory yeast strains, facilitates both the de novo formation and destabilization of other yeast prions, and affects aggregation and toxicity of human misfolding disease proteins expressed in yeast.

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