ArticleMolecular biology of the cell2010
Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.
Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 47 citations in OpenAlex.
- Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2025Article
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- Article
- Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons.International journal of molecular sciences · 2020Review
- Aggregation and Prion-Inducing Properties of the G-Protein Gamma Subunit Ste18 are Regulated by Membrane Association.International journal of molecular sciences · 2020Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Toxicity and infectivity: insights from de novo prion formation.Current genetics · 2018Review
- The Insoluble Protein Deposit (IPOD) in Yeast.Frontiers in molecular neuroscience · 2018Article
- Study of Amyloids Using Yeast.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Disrupting the cortical actin cytoskeleton points to two distinct mechanisms of yeast [PSI+] prion formation.PLoS genetics · 2017Article
- Analysis of [SWIMolecular microbiology · 2017Article
- De novo [PSIScientific reports · 2017Article
- Autophagy protects against de novo formation of the [PSI+] prion in yeast.Molecular biology of the cell · 2015Article
- Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.Molecular microbiology · 2015Article
- Heterologous aggregates promote de novo prion appearance via more than one mechanism.PLoS genetics · 2015Article
- Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeleton.Molecular cell · 2014Article
- Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiae.Prion · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Various proteins, like the infectious yeast prions and the noninfectious human Huntingtin protein (with expanded polyQ), depend on a Gln or Asn (QN)-rich region for amyloid formation. Other prions, e.g., mammalian PrP and the [Het-s] prion of Podospora anserina, although still able to form infectious amyloid aggregates, do not have QN-rich regions. Furthermore, [Het-s] and yeast prions appear to differ dramatically in their amyloid conformation. Despite these differences, a fusion of the Het-s prion domain to GFP (Het-sPrD-GFP) can propagate in yeast as a prion called [Het-s](y). We analyzed the properties of two divergent prions in yeast: [Het-s](y) and the native yeast prion [PSI(+)] (prion form of translational termination factor Sup35). Curiously, the induced appearance and transmission of [PSI(+)] and [Het-s](y) aggregates is remarkably similar. Overexpression of tagged prion protein (Sup35-GFP or Het-sPrD-GFP) in nonprion cells gives rise to peripheral, and later internal, ring/mesh-like aggregates. The cells with these ring-like aggregates give rise to daughters with one (perivacuolar) or two (perivacuolar and juxtanuclear) dot-like aggregates per cell. These line, ring, mesh, and dot aggregates are not really the transmissible prion species and should only be regarded as phenotypic markers of the presence of the prions. Both [PSI(+)] and [Het-s](y) first appear in daughters as numerous tiny dot-like aggregates, and both require the endocytic protein, Sla2, for ring formation, but not propagation.
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