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Creutzfeldt-Jakob disease and mad cows: lessons learnt from yeast cells

J Hofmann1, H Wolf, A Grassmann

  • 1Deutsches Zentrum für Neurodegenerative Erkrankungen e.V., Bonn, Germany. julia.hofmann@dzne.de

Swiss Medical Weekly
|January 25, 2012
PubMed

Insights

Yeast prions, aggregates of misfolded proteins, mimic mammalian prion diseases. These lower eukaryote prions offer insights into prion formation and protein-based epigenetic inheritance.

Area of Science:

  • Neurobiology
  • Molecular Biology
  • Genetics

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases.
  • Prion diseases are caused by misfolded host proteins (PrP).
  • Studies in yeast and fungi have revealed insights into prion propagation.

Purpose of the Study:

  • To explore the role of yeast prions as models for mammalian prion diseases.
  • To understand prion biogenesis and protein-based epigenetic inheritance.

Main Methods:

  • Investigating the structure and propagation of misfolded proteins in yeast.
  • Comparing mechanisms of prion formation in lower eukaryotes and mammals.

Main Results:

  • Yeast prions, composed of misfolded proteins, propagate via conformational changes.
  • These prions act as epigenetic elements, transmitting alternative protein states.
  • Yeast prions demonstrate that distinct protein conformers can be infectious and encode strain information.

Conclusions:

  • Yeast prions serve as a tractable model system for studying prion diseases.
  • Yeast prions provide crucial insights into prion biogenesis and protein-based epigenetic inheritance.
  • Further research using yeast prions will enhance understanding of prion-host interactions.

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