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Updated: Jul 14, 2026
08:12
High-throughput Screening for Protein-based Inheritance in S. cerevisiae
Published on: August 8, 2017
Stress and prions: lessons from the yeast model
1School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0230, USA. yury.chernoff@biology.gatech.edu
FEBS Letters
|May 19, 2007
Summary
Yeast prions, which are self-replicating amyloids, are influenced by chaperone proteins like Hsp104. Cellular stress can impact prion formation and loss, suggesting a protective role for these protein aggregates.
Area of Science:
- Cellular biology
- Biochemistry
- Protein aggregation
Background:
- Yeast prions (self-perpetuating amyloids) serve as models for mammalian protein assembly disorders.
- Amyloid propagation in yeast depends on interactions with specific cellular machinery.
Purpose of the Study:
- To investigate the role of cellular factors in yeast prion formation and propagation.
- To understand the influence of stress conditions and chaperone networks on prion dynamics.
Main Methods:
- Utilized yeast as a model system for prion studies.
- Examined the impact of chaperone proteins (Hsp104, Hsp70, Hsp40) on prion propagation.
- Investigated the effects of protein trafficking and degradation networks.
Main Results:
- Hsp104 chaperone is critical for yeast prion propagation.
- Other stress-related chaperones (Hsp70, Hsp40) and cellular networks affect prion formation and loss.
- Specific stress conditions can induce or abolish prions.
Conclusions:
- Yeast prions are influenced by chaperone interactions and cellular networks.
- Prions may function as protective byproducts of protein assembly under stress.
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