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- Introduction
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1. Prions and amyloids: introduction
- Prof. Reed Wickner
- Mammalian Prions
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2. Transgenic mouse models of prion diseases
- Prof. Glenn Telling
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3. Mechanism of prion generation in vitro
- Dr. Surachai Supattapone
- Non-Prion Amyloids
- Yeast Prions
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6. Chaperones and prions
- Prof. Yury Chernoff
- Beneficial Amyloids
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7. The dark side of amyloid: PMEL, a natural amyloid in melanosome biogenesis
- Prof. Michael Marks
- Archived Lectures *These may not cover the latest advances in the field
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8. Predicting TSE transmission
- Prof. Jean Manson
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10. Yeast and fungal prions: a help or a hindrance?
- Prof. Reed Wickner
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11. [PIN+]: prions beget prions
- Prof. Susan Liebman
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12. Yeast prions and protein chaperones
- Dr. Daniel Masison
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13. Mechanisms of yeast prion propagation
- Prof. Mick Tuite
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14. Propagation and variability of the yeast [PSI+] prion
- Prof. Michael Ter-Avanesyan
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15. The genetics and biology of the [Het-s] prion of Podospora
- Prof. Sven Saupe
Printable Handouts
Navigable Slide Index
- Introduction
- Prions
- What is [PSI+]?
- Domain structure of the Sup35 (eRF3) protein
- Suppression of the ade2 nonsense mutations
- Nonsense suppression by Sup35 overproduction
- [PSI+] curing by overproduced chaperones
- Hsp104 chaperone level and [PSI+] curing
- Effect of Hsp104 excess on Sup35
- Polymerization-fragmentation model
- [PSI+] prion particles contain Sup35 polymers
- Hsp104 depletion affects size of Sup35 polymers
- Effet of GuHCl on size of Sup35 polymers
- [PSI+] and Hsp104: conclusions
- Continuous Sup35 overproduction
- Sup35 multicopy suppression and [PSI+]
- Observations
- Sup35 levels and nonsense codon readthrough
- Continuous Sup35 overproduction: conclusions
- PolyQ/QY proteins polymerization in [PIN+] cells
- Differences between [PSI+] variants
- Sup35 N domain
- [PSI+] transmission from WT to mutant Sup35 (1)
- Results of Sup35 PrD repeats deletion
- [PSI+] transmission by truncated Sup35 mutants
- [PSI+] transmission from WT to mutant Sup35 (2)
- Co-expression of wild-type and mutant Sup35
- Effect of the co-expression on polymers size
- Prion fold and insertion of Sup35 WT/mutant
- Sup35 truncations analysis: conclusions
- Acknowledgements
Topics Covered
- Prion
- Yeast prions as non-chromosomal genetic determinants
- Modular structure of the Sup35 protein responsible for the yeast [PSI+] prion
- Role of the Hsp104 chaperone in [PSI+] prion propagation
- Two-level structure of the [PSI+] prion aggregates and methods for studying the size of prion polymers
- Non-prion amyloids in yeast
- Variability of the yeast [PSI+] prion
Talk Citation
Ter-Avanesyan, M. (2008, September 4). Propagation and variability of the yeast [PSI+] prion [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved October 11, 2024, from https://doi.org/10.69645/UKYB5766.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Michael Ter-Avanesyan has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.