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Related Experiment Video

Updated: Jun 10, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Prion amyloid structure explains templating: how proteins can be genes.

Reed B Wickner¹, Frank Shewmaker, Herman Edskes

¹Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA. wickner@helix.nih.gov

FEMS Yeast Research

|August 24, 2010

Summary

Yeast prions are protein-based genes that form amyloid structures. Their in-register parallel architecture explains protein inheritance and templating, though prion formation is often disadvantageous.

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Published on: January 8, 2015

Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Prions are protein-based genes that confer heritable traits in yeast and fungi.
These proteins form amyloid structures, which are filamentous polymers rich in beta-sheets.
A single prion protein sequence can generate multiple, distinct inherited variants (alleles).

Purpose of the Study:

To elucidate the protein structure responsible for prion-based inheritance.
To understand the templating mechanism of prion amyloid filaments.

Main Methods:

Solid-state nuclear magnetic resonance (ssNMR) spectroscopy was employed.
The study focused on the prion domains of Ure2p, Sup35p, and Rnq1p proteins in yeast.

Main Results:

The infectious amyloids of Ure2p, Sup35p, and Rnq1p exhibit an in-register parallel architecture.
This specific structure facilitates the templating of new protein molecules at filament ends.
Prion formation is not conserved and often detrimental to yeast cells, suggesting it represents a disease state.

Conclusions:

The in-register parallel architecture of prion amyloids is key to protein-based inheritance.
Prion domains have functions independent of prion formation.
Prion formation is rare, potentially a disease, with evolutionary mechanisms limiting transmission.