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We present methods to prepare infectious Sup35 protein aggregates and use them for genetic transformation of yeast. The protein aggregates are prepared from bacterially expressed recombinant protein, which is converted to amyloid fibers by extended incubation or by nucleated growth using yeast prion particles as seeds. The aggregates are introduced into yeast by a modified spheroplast transformation...
The [PSI + ] prion of the yeast Saccharomyces cerevisiae was first identified by Brian Cox some 40 years ago as a non-Mendelian genetic element that modulated the efficiency of nonsense suppression. Following the suggestion by Reed Wickner in 1994 that such elements might be accounted for by invoking a prion-based model, it was subsequently established that the [PSI + ] determinant...
Recently, we have developed a yeast-based (Saccharomyces cerevisiae) assay to isolate drugs active against mammalian prions. The initial assumption was that mechanisms controlling prion appearance and/or propagation could be conserved from yeast to human, as it is the case for most of the major cell biology regulatory mechanisms. Indeed, the vast majority of drugs we isolated as active against both...
The glutamine- and asparagine-rich Rnq1p protein in Saccharomyces cerevisiae can exist in the cell as a soluble monomer or in one of several aggregated, infectious, prion forms called [PIN + ]. Interest in [PIN + ] is heightened by its ability to promote the conversion of other proteins into a prion or an aggregated amyloid state. However, little is known about the function of Rnq1p,...
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