ArticleMolecular cell2007
A non-Q/N-rich prion domain of a foreign prion, [Het-s], can propagate as a prion in yeast.
Article in Molecular cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 90 citations in OpenAlex.
- Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis.Communications biology · 2022Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
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- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
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- Study of Amyloids Using Yeast.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Q-Rich Yeast Prion [Frontiers in molecular neuroscience · 2018Article
- Article
- The HET-S/s Prion Motif in the Control of Programmed Cell Death.Cold Spring Harbor perspectives in biology · 2016Review
- Overlapping Podospora anserina Transcriptional Responses to Bacterial and Fungal Non Self Indicate a Multilayered Innate Immune Response.Frontiers in microbiology · 2016Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold.PLoS biology · 2015Article
- Article
- Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Rebels with a cause: molecular features and physiological consequences of yeast prions.FEMS yeast research · 2014Review
- Soluble oligomers are sufficient for transmission of a yeast prion but do not confer phenotype.The Journal of cell biology · 2013Article
- Prions in yeast.Genetics · 2012Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
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.
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Registered trials
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