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• W2099661489 startingPage "866" @default.
• W2099661489 abstract "Differences in the clinical pathology of mammalian prion diseases reflect distinct heritable conformations of aggregated PrP proteins, called prion strains. Here, using the yeast [PSI(+) ] prion, we examine the de novo establishment of prion strains (called variants in yeast). The [PSI(+) ] prion protein, Sup35, is efficiently induced to take on numerous prion variant conformations following transient overexpression of Sup35 in the presence of another prion, e.g. [PIN(+) ]. One hypothesis is that the first [PSI(+) ] prion seed to arise in a cell causes propagation of only that seed's variant, but that different variants could be initiated in different cells. However, we now show that even within a single cell, Sup35 retains the potential to fold into more than one variant type. When individual cells segregating different [PSI(+) ] variants were followed in pedigrees, establishment of a single variant phenotype generally occurred in daughters, granddaughters or great-granddaughters - but in 5% of the pedigrees cells continued to segregate multiple variants indefinitely. The data are consistent with the idea that many newly formed prions go through a maturation phase before they reach a single specific variant conformation. These findings may be relevant to mammalian PrP prion strain establishment and adaptation." @default.
• W2099661489 created "2016-06-24" @default.
• W2099661489 creator A5000551077 @default.
• W2099661489 creator A5073859263 @default.
• W2099661489 date "2012-09-24" @default.
• W2099661489 modified "2023-10-01" @default.
• W2099661489 title "[<i>PSI</i>⁺] prion variant establishment in yeast" @default.
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• W2099661489 doi "https://doi.org/10.1111/mmi.12024" @default.
• W2099661489 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3543502" @default.
• W2099661489 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22998111" @default.
• W2099661489 hasPublicationYear "2012" @default.
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