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• W2168373973 endingPage "2443" @default.
• W2168373973 startingPage "2433" @default.
• W2168373973 abstract "The [PSI(+)] prion is the aggregated self-propagating form of the Sup35 protein from the yeast Saccharomyces cerevisiae. Aggregates of Sup35 in [PSI(+)] cells exist in different heritable conformations, called variants, and they are composed of detergent-resistant Sup35 polymers, which may be closely associated with themselves, other proteins, or both. Here, we report that disassembly of the aggregates into individual Sup35 polymers and non-Sup35 components increases their infectivity while retaining their variant specificity, showing that variant-specific [PSI(+)] infection can be transmitted by Sup35 polymers alone. Morphological analysis revealed that Sup35 isolated from [PSI(+)] yeast has the appearance of short barrels, and bundles, which seem to be composed of barrels. We show that the major components of two different variants of [PSI(+)] are interacting infectious Sup35 polymers and Ssa1/2. Using a candidate approach, we detected Hsp104, Ssb1/2, Sis1, Sse1, Ydj1, and Sla2 among minor components of the aggregates. We demonstrate that Ssa1/2 efficiently binds to the prion domain of Sup35 in [PSI(+)] cells, but that it interacts poorly with the nonaggregated Sup35 found in [psi(-)] cells. Hsp104, Sis1, and Sse1 interact preferentially with the prion versus nonprion form of Sup35, whereas Sla2 and Ssb1/2 interact with both forms of Sup35 with similar efficiency." @default.
• W2168373973 created "2016-06-24" @default.
• W2168373973 creator A5022502578 @default.
• W2168373973 creator A5067251751 @default.
• W2168373973 creator A5068311626 @default.
• W2168373973 creator A5073859263 @default.
• W2168373973 date "2008-06-01" @default.
• W2168373973 modified "2023-09-23" @default.
• W2168373973 title "Variant-specific [<i>PSI</i>⁺] Infection Is Transmitted by Sup35 Polymers within [<i>PSI</i>⁺] Aggregates with Heterogeneous Protein Composition" @default.
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