Ontology highlight
ABSTRACT:
SUBMITTER: Taneja V
PROVIDER: S-EPMC1995001 | biostudies-literature | 2007 Jul
REPOSITORIES: biostudies-literature
Taneja Vibha V Maddelein Marie-Lise ML Talarek Nicolas N Saupe Sven J SJ Liebman Susan W SW
Molecular cell 20070701 1
Prions are self-propagating, infectious aggregates of misfolded proteins. The mammalian prion, PrP(Sc), causes fatal neurodegenerative disorders. Fungi also have prions. While yeast prions depend upon glutamine/asparagine (Q/N)-rich regions, the Podospora anserina HET-s and PrP prion proteins lack such sequences. Nonetheless, we show that the HET-s prion domain fused to GFP propagates as a prion in yeast. Analogously to native yeast prions, transient overexpression of the HET-s fusion induces ri ...[more]