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Updated: Jun 4, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
Prion diseases of yeast: amyloid structure and biology
Reed B Wickner1, Herman K Edskes, Dmitry Kryndushkin
1Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, United States. wickner@helix.nih.gov
Abstract:
Prion "variants" or "strains" are prions with the identical protein sequence, but different characteristics of the prion infection: e.g. different incubation periods for scrapie strains or different phenotype intensities for yeast prion variants. We have shown that infectious amyloids of the yeast prions [PSI+], [URE3] and [PIN+] each have an in-register parallel β-sheet architecture. Moreover, we have pointed out that this amyloid architecture can explain how one protein can faithfully transmit any of several conformations to new protein monomers. This explains how proteins can be genes.
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