Unknown

Dataset Information

0

A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.


ABSTRACT: 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 ring-like aggregates that propagate in daughter cells as cytoplasmically inherited, detergent-resistant dot aggregates. Efficient dot propagation, but not ring formation, is dependent upon the Hsp104 chaperone. The yeast prion [PIN(+)] enhances HET-s ring formation, suggesting that prions with and without Q/N-rich regions interact. Finally, HET-s aggregates propagated in yeast are infectious when introduced into Podospora. Taken together, these results demonstrate prion propagation in a truly foreign host. Since yeast can host non-Q/N-rich prions, such native yeast prions may exist.

SUBMITTER: Taneja V 

PROVIDER: S-EPMC1995001 | biostudies-literature | 2007 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.

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]

Similar Datasets

| S-EPMC2667906 | biostudies-literature
| S-EPMC4262963 | biostudies-literature
| S-EPMC3531502 | biostudies-literature
| S-EPMC2920664 | biostudies-literature
| S-EPMC5859028 | biostudies-literature
| S-EPMC3795258 | biostudies-literature
| S-EPMC3507513 | biostudies-literature
| S-EPMC7526898 | biostudies-literature
| S-EPMC9312190 | biostudies-literature
| S-EPMC1800594 | biostudies-literature