Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.

Abstract excerpt

Yeast prions are self-templating protein-based mechanisms of inheritance whose conformational changes lead to the acquisition of diverse new phenotypes. The best studied of these is the prion domain (NM) of Sup35, which forms an amyloid that can adopt several distinct conformations (strains) that confer distinct phenotypes when introduced into cells that do not carry the prion. Here, we investigate the structure...

Topics

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• Amyloid
• Microscopy, Electron, Scanning
• Nuclear Magnetic Resonance, Biomolecular
• Peptide Termination Factors
• Prions