Genetic and Environmental Factors Affecting the de novo Appearance of the [PSI + ] Prion in Saccharomyces cerevisiae (original) (raw)

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Laboratory for Molecular Biology

, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607

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Laboratory for Molecular Biology

, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607

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,

Laboratory for Molecular Biology

, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607

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,

School of Biology

, Georgia Institute of Technology, Atlanta, Georgia 30332-0230

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Laboratory for Molecular Biology

, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607

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Published:

01 October 1997

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Irina L Derkatch, Michael E Bradley, Ping Zhou, Yury O Chernoff, Susan W Liebman, Genetic and Environmental Factors Affecting the de novo Appearance of the [PSI + ] Prion in Saccharomyces cerevisiae, Genetics, Volume 147, Issue 2, 1 October 1997, Pages 507–519, https://doi.org/10.1093/genetics/147.2.507
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It has previously been shown that yeast prion [PSI + ] is cured by GuHCl, although reports on reversibility of curing were contradictory. Here we show that GuHCl treatment of both [PSI + ] and [psi – ] yeast strains results in two classes of [psi – ] derivatives: Pin+, in which [PSI + ] can be reinduced by Sup35p overproduction, and Pin–, in which overexpression of the complete SUP35 gene does not lead to the [PSI + ] appearance. However, in both Pin+ and Pin– derivatives [PSI + ] is reinduced by overproduction of a short Sup35p N-terminal fragment, thus, in principle, [PSI + ] curing remains reversible in both cases. Neither suppression nor growth inhibition caused by SUP35 overexpression in Pin+ [psi – ] derivatives are observed in Pin– [psi – ] derivatives. Genetic analyses show that the Pin+ phenotype is determined by a non-Mendelian factor, which, unlike the [PSI + ] prion, is independent of the Sup35p N-terminal domain. A Pin– [psi – ] derivative was also generated by transient inactivation of the heat shock protein, Hsp104, while [PSI + ] curing by Hsp104 overproduction resulted exclusively in Pin+ [psi – ] derivatives. We hypothesize that in addition to the [PSI + ] prion-determining domain in the Sup35p N-terminus, there is another self-propagating conformational determinant in the C-proximal part of Sup35p and that this second prion is responsible for the Pin+ phenotype.

Communicating editor: F. Winston

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© Genetics 1997

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