Registration for a live webinar on 'Precision medicine treatment for anticancer drug resistance' is now open.
See webinar detailsWe noted you are experiencing viewing problems
-
Check with your IT department that JWPlatform, JWPlayer and Amazon AWS & CloudFront are not being blocked by your network. The relevant domains are *.jwplatform.com, *.jwpsrv.com, *.jwpcdn.com, jwpltx.com, jwpsrv.a.ssl.fastly.net, *.amazonaws.com and *.cloudfront.net. The relevant ports are 80 and 443.
-
Check the following talk links to see which ones work correctly:
Auto Mode
HTTP Progressive Download Send us your results from the above test links at access@hstalks.com and we will contact you with further advice on troubleshooting your viewing problems. -
No luck yet? More tips for troubleshooting viewing issues
-
Contact HST Support access@hstalks.com
-
Please review our troubleshooting guide for tips and advice on resolving your viewing problems.
-
For additional help, please don't hesitate to contact HST support access@hstalks.com
We hope you have enjoyed this limited-length demo
This is a limited length demo talk; you may
login or
review methods of
obtaining more access.
Printable Handouts
Navigable Slide Index
- Introduction
- Definition of 'epigenetics'
- Non-chromosomal components of yeast genome
- Inheritance vs. infection
- Prions: definition and classification
- [URE3] and [PSI] as prions
- Genetic criteria for a prion: illustrated with [URE3]
- Prion domain of Ure2p
- Comparison of prion domains
- Amyloid: a pathogenic protein form
- Amyloid of Ure2p is the basis of the [URE3] prion
- Ure2p filaments are present only in [URE3] cells
- Architecture of Ure2p amyloid filaments
- Ure2p C-terminal domain
- Shuffling of Ure2 prion domain
- Sequence independence of prion domain
- In-register structure explains prion properties
- Amyloid assembly by Ure2p
- Ure2 from pathogenic yeasts
- Chaperones and prions
- Prion variants and species barrier
- Prion strain affects species barrier
- Infection with prions by introduction of amyloid
- Heterokaryon incompatibility
- [Het-s] and meiotic drive
- Yeast prions: help or hindrance
- Selfish RNAs, DNAs and prions
- Major challenges for prion research
- References (1)
- References (2)
Topics Covered
- Prions (infectious proteins) include several self-propagating amyloids of S. cerevisiae and Podospora anserina and a self-activating enzyme of S. cerevisiae
- these non-chromosomal genetic elements are genes composed of protein, just as nucleic acids can catalyse enzymatic reactions
- the amyloid-based prions [PSI+] and [URE3] are diseases of yeast, but the [Het-s] prion of Podospora carries out a normal function for that organism, heterokaryon incompatibility
Talk Citation
Wickner, R. (2007, October 1). Cytoplasmic epigenetics: proteins acting as genes [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved December 26, 2024, from https://doi.org/10.69645/PCIC8234.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Reed Wickner has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.