Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies

Rupam Ghosh, Jijun Dong, Joe Wall, Kendra K. Frederick

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


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 of NM fibrils templated into the prion conformation with cellular lysates. Our electron microscopy studies reveal that NM fibrils that confer either a strong or a weak prion phenotype are both mixtures of thin and thick fibrils that result from differences in packing of the M domain. Strong NM fibrils have more thin fibrils and weak NM fibrils have more thick fibrils. Interestingly, both mass per length and solid state NMR reveal that the thin and thick fibrils have different underlying molecular structures in the prion strain variants that do not interconvert.

Original languageEnglish (US)
Article numberfoy059
JournalFEMS Yeast Research
Issue number6
StatePublished - Sep 1 2018


  • Amyloid
  • Prion
  • Prion strains
  • Scanning transmission electron microscopy (STEM)
  • Solid-state nuclear magnetic resonance (NMR)
  • Structural biology
  • Sup35

ASJC Scopus subject areas

  • Microbiology
  • Applied Microbiology and Biotechnology


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