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The genetics and biology of the [Het-s] prion of Podospora
- Author / Creator
- Available as
- Online
- Summary
-
Audio-visual presentation: Mammalian prions -- Fungal prions -- Yeast: [URE3], [PSI+] and [PIN+] -- Filamentous fungi: [Het-s] -- Fungal self non-self recognition -- Heterokaryon incompatibility --...
Audio-visual presentation: Mammalian prions -- Fungal prions -- Yeast: [URE3], [PSI+] and [PIN+] -- Filamentous fungi: [Het-s] -- Fungal self non-self recognition -- Heterokaryon incompatibility -- Genetics of [Het-s] -- Maternal inheritance -- Meiotic drive -- In vivo and in vitro aggregation of HET-s protein -- Role of the Hsp104 chaperone in [Het-s] system -- Role of the Hsp104 chaperone in [Het-s] prion propagation -- Podospora anserine.
Details
- Creator
- Sven Saupe
- Format
- Videos, Slides, Films
- Language
- English
- Publication
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- London : Henry Stewart Talks, 2008
- Physical Details
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- 1 videorecording (42 min., 46 sec.) : sound, color
- video file
- Retrieved April 19, 2024, from https://hstalks.com/bs/964/.
- Introduction -- Prion definition -- Outline -- Filamentous fungi form coenocytic structures -- Filamentous fungi undergo somatic cell fusion -- Heterokaryon incompatibility -- Genetics of incompatibility -- Proposed function of heterokaryon incompatibility -- Positive Darwinian selection on het loci -- The barrage reaction -- The Het-s system (1) -- The Het-s system (2) -- Propagation of Het-s -- [Het-s] shows strict maternal inheritance -- [Het-s] is lost in het-s x het-S crosses -- The het-S spore killing phenomenon -- HET-s and HET-S differ by 13 amino acids -- HET-s aggregates in vivo -- HET-s forms self-perpetuating aggregates in vitro -- HET-s aggregates are amyloids (1) -- HET-s aggregates are amyloids (2) -- HET-s amyloids display prion infectivity (1) -- HET-s amyloids display prion infectivity (2) -- HET-s amyloids display prion infectivity (3) -- Proteinase K resistant HET-s amyloids core -- Identification of pK resistant fragment -- HET-s prion forming domain -- Het-s prion forming domain in GFP fusion -- HET-s structural transition analyses by HXMS (1) -- Het-s structural transition analyses by HXMS (2) -- Het-s structural transition analyses by HXMS (3) -- Domain organisation of HET-s -- Elongated Het-s 157-289 aggregates -- Time lapse of Het-s 157-289 aggregate formation -- In vivo EM of HET-s 157-289 aggregates -- Het-s (218-289) structure (1) -- Het-s (218-289) structure (2) -- Het-s (218-289) structure (3) -- Het-s (218-289) model -- Het-s (218-289) structure-function correlation (1) -- Het-s (218-289) structure-function correlation (2) -- STEM and electron diffraction of HET-s fibrils -- Prion and non-prion Het-s (218) amyloids (1) -- Prion and non-prion Het-s (218) amyloids (2) -- Prion and non-prion Het-s (218) amyloids (3) -- Prion and non-prion Het-s (218) amyloids (4) -- Prion and non-prion Het-s (218) amyloids (5) -- Hsp104 chaperone role in Het-s prion propagation -- PaHsp104 required for Podospora thermotolerance -- Het-s propagated in the absence of PaHsp105 -- PaHsp104 inactivation reduces # propagons -- PaHsp104 inactivation reduces propagation rate -- PaHsp104 inactivation and aggregates morphology -- PaHsp104 inactivation effect during sexual cycle -- Het-s propagation in yeast (1) -- Het-s propagation in yeast (2) -- Summary -- Comparison between Het-s and yeast prions -- Open question (1) -- Open question (2) -- Acknowledgements -- References