ArticleMolecular microbiology2014
Extracellular environment modulates the formation and propagation of particular amyloid structures.
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.
- Origin of life: β-sheet amyloid conformers as the primordial functional polymers on the early Earth and their role in the emergence of complex dynamic networks.FEBS letters · 2025Review
- Nucleation seed size determines amyloid clearance and establishes a barrier to prion appearance in yeast.Nature structural & molecular biology · 2020Article
- Protein Supramolecular Structures: From Self-Assembly to Nanovaccine Design.Nanomaterials (Basel, Switzerland) · 2020Review
- Client processing is altered by novel myopathy-causing mutations in the HSP40 J domain.PloS one · 2020Article
- Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-like Phase Behavior.Molecular cell · 2018Article
- Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.Cellular and molecular life sciences : CMLS · 2018Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae.Scientific reports · 2017Article
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.PLoS genetics · 2014Article
- 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
Corrections and comments
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Authors and funding
2 authors.
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Abstract
Amyloidogenic proteins, including prions, assemble into multiple forms of structurally distinct fibres. The [PSI(+)] prion, endogenous to the yeast Saccharomyces cerevisiae, is a dominantly inherited, epigenetic modifier of phenotypes. [PSI(+)] formation relies on the coexistence of another prion, [RNQ(+)]. Here, in order to better define the role of amyloid diversity on cellular phenotypes, we investigated how physiological and environmental changes impact the generation and propagation of diverse protein conformations from a single polypeptide. Utilizing the yeast model system, we defined extracellular factors that influence the formation of a spectrum of alternative self-propagating amyloid structures of the Sup35 protein, called [PSI(+)] variants. Strikingly, exposure to specific stressful environments dramatically altered the variants of [PSI(+)] that formed de novo. Additionally, we found that stress also influenced the association between the [PSI(+)] and [RNQ(+)] prions in a way that it superceded their typical relationship. Furthermore, changing the growth environment modified both the biochemical properties and [PSI(+)]-inducing capabilities of the [RNQ(+)] template. These data suggest that the cellular environment contributes to both the generation and the selective propagation of specific amyloid structures, providing insight into a key feature that impacts phenotypic diversity in yeast and the cross-species transmission barriers characteristic of prion diseases.
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