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Related Experiment Video

Updated: Jul 18, 2026

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Ageing in yeast does not enhance prion generation.

Frank Shewmaker1, Reed B Wickner

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, USA.

Yeast (Chichester, England)
|November 30, 2006
PubMed
Summary

Yeast prions [URE3] and [PSI(+)] are amyloid proteins. Researchers found that aging yeast cells do not increase the spontaneous generation of these prions, challenging assumptions about age-related prion diseases.

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Last Updated: Jul 18, 2026

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Area of Science:

  • Molecular Biology
  • Prion Biology
  • Aging Research

Background:

  • Yeast prions [URE3] and [PSI(+)] are self-propagating protein aggregates (amyloids) of Ure2p and Sup35p.
  • Mammalian transmissible spongiform encephalopathies and other amyloidoses are often associated with later life.

Purpose of the Study:

  • To investigate whether yeast cell aging influences the spontaneous generation of prions.
  • To determine if aging increases the frequency of de novo prion occurrence in yeast.

Main Methods:

  • Isolation of old yeast cells from normal strains lacking prions.
  • Measurement of the frequency of de novo [URE3] and [PSI(+)] prion generation in aged cells.

Main Results:

  • No evidence was found to suggest that aging increases the frequency of prion occurrence in yeast.
  • The rate of spontaneous prion formation remained consistent regardless of cell age.

Conclusions:

  • Yeast aging does not appear to be a significant factor in the de novo generation of [URE3] and [PSI(+)] prions.
  • This finding has implications for understanding the role of aging in prion diseases across different organisms.