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Published on: August 8, 2017
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Yeast prions: structure, biology, and prion-handling systems
Reed B Wickner1, Frank P Shewmaker2, David A Bateman3
1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA wickner@helix.nih.gov.
Microbiology and Molecular Biology Reviews : MMBR
|January 30, 2015
Summary
Yeast and fungal prions are infectious proteins that propagate by altering protein shape. These protein-based genes, or prions, serve as models for human amyloid diseases, offering insights into disease mechanisms and potential treatments.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- Prions are infectious proteins that transmit traits without nucleic acids.
- Yeast and fungal prions are protein-only genes, often involving altered proteins that catalyze further alterations.
- Amyloid formation, characterized by ordered β-sheet-rich aggregates, is fundamental to most yeast and fungal prions.
Purpose of the Study:
- To review the mechanisms of prion templating and biological roles.
- To explore prion interactions with cellular chaperones and aggregate-handling systems.
- To highlight yeast prions as models for understanding and treating human amyloidoses.
Main Methods:
- Review of existing literature on prion biology.
- Analysis of prion propagation mechanisms, including faithful templating of protein conformation.
- Examination of cellular factors, such as chaperones (Btn2, Cur1), involved in prion management.
Main Results:
- Prion proteins can exist in multiple self-propagating amyloid forms (prion variants) with distinct properties.
- Cellular chaperones and specific aggregate-handling systems play crucial roles in prion generation and propagation.
- Yeast prions exhibit both vertical (as genes) and horizontal (as infectious agents) transmission.
Conclusions:
- Yeast prions provide valuable models for studying mammalian amyloidoses, including human prion diseases and other amyloid-based conditions.
- Understanding prion variants in yeast may offer insights into the diverse clinical presentations of human amyloidoses.
- Research into yeast prions can inform the development of therapeutic strategies for amyloid-related diseases.
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