ArticleMolecular microbiology2014
Wild yeast harbour a variety of distinct amyloid structures with strong prion-inducing capabilities.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Transcriptomic analysis of Rnq1 loss and prionization reveals alterations in translation pathways and energy metabolism.Scientific reports · 2026Article
- Cellular Stress Impact on Yeast Activity in Biotechnological Processes-A Short Overview.Microorganisms · 2023Review
- The Cellular Prion Protein-ROCK Connection: Contribution to Neuronal Homeostasis and Neurodegenerative Diseases.Frontiers in cellular neuroscience · 2021Review
- SUMO and cellular adaptive mechanisms.Experimental & molecular medicine · 2020Review
- A complete catalog of wild-type Sup35 prion variants and their protein-only propagation.Current genetics · 2020Article
- Baker's Yeast Clinical Isolates Provide a Model for How Pathogenic Yeasts Adapt to Stress.Trends in genetics : TIG · 2019Review
- Article
- Independent amplification of co-infected long incubation period low conversion efficiency prion strains.PLoS pathogens · 2018Article
- Using High Performance Thin Layer Chromatography-Densitometry to Study the Influence of the Prion [Separations · 2018Article
- Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.PLoS genetics · 2016Article
- Prion strains and amyloid polymorphism influence phenotypic variation.PLoS pathogens · 2014Review
- Structural variants of yeast prions show conformer-specific requirements for chaperone activity.Molecular microbiology · 2014Article
- Myopathy-causing mutations in an HSP40 chaperone disrupt processing of specific client conformers.The Journal of biological chemistry · 2014Article
- Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.PLoS genetics · 2014Article
- Extracellular environment modulates the formation and propagation of particular amyloid structures.Molecular microbiology · 2014Article
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2 authors.
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Abstract
Variation in amyloid structures profoundly influences a wide array of pathological phenotypes in mammalian protein conformation disorders and dominantly inherited phenotypes in yeast. Here, we describe, for the first time, naturally occurring, self-propagating, structural variants of a prion protein isolated from wild strains of the yeast Saccharomyces cerevisiae. Variants of the [RNQ⁺] prion propagating in a variety of wild yeast differ biochemically, in their intracellular distributions, and in their ability to promote formation of the [PSI⁺] prion. [PSI⁺] is an epigenetic regulator of cellular phenotype and adaptability. Strikingly, we find that most natural [RNQ⁺] variants induced [PSI⁺] at high frequencies and the majority of [PSI⁺] variants elicited strong cellular phenotypes. We hypothesize that the presence of an efficient [RNQ⁺] template primes the cell for [PSI⁺] formation in order to induce [PSI⁺] in conditions where it would be advantageous. These studies utilize naturally occurring structural variants to expand our understanding of the consequences of diverse prion conformations on cellular phenotypes.
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