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PMID: 17612491 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

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

Molecular cell ·Vol. 27 ·No. 1 ·2007-07-06 ·Pages 67-77

Taneja V, Maddelein ML, Talarek N, Saupe SJ, Liebman SW

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.

MeSH Terms
Asparagine/analysis Detergents/pharmacology Gene Deletion Glutamine/analysis Heat-Shock Proteins/metabolism Podospora/chemistry,drug effects Prions/chemistry,metabolism Protein Structure, Quaternary Protein Structure, Tertiary Recombinant Fusion Proteins/metabolism Saccharomyces cerevisiae/cytology,drug effects,metabolism Saccharomyces cerevisiae Proteins/metabolism Sarcosine/analogs & derivatives,pharmacology
Chemicals
Detergents Heat-Shock Proteins Prions Recombinant Fusion Proteins Saccharomyces cerevisiae Proteins Glutamine HsP104 protein, S cerevisiae sarkosyl Asparagine Sarcosine
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Taneja Vibha
Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607, USA.
Maddelein Marie-Lise
Talarek Nicolas
Saupe Sven J
Liebman Susan W
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Article Info
Journal
Molecular cell
Abbr.
Mol Cell
ISSN
1097-2765
DOI
10.1016/j.molcel.2007.05.027
Published
2007-07-06
Pages
67-77
Language
English
Region
United States
NLM ID
9802571
PMCID
PMC1995001
Subset
IM
Grants
NIGMS NIH HHS · R01 GM056350 · United States
NIGMS NIH HHS · R01 GM056350-10 · United States
External Links
PubMed source DOI: 10.1016/j.molcel.2007.05.027 PMC Full Text View journal details
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