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

INVESTIGATIONS

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

I. L. Derkatch, M. E. Bradley, P. Zhou, Y. O. Chernoff and S. W. Liebman
Laboratory for Molecular Biology, Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois 60607

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.

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				C.-Y. Chen, K. Rojanatavorn, A. C. Clark, and J. C.H. Shih Characterization and enzymatic degradation of Sup35NM, a yeast prion-like protein Protein Sci., September 1, 2005; 14(9): 2228 - 2235. [Abstract] [Full Text] [PDF]

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				A. B. Salnikova, D. S. Kryndushkin, V. N. Smirnov, V. V. Kushnirov, and M. D. Ter-Avanesyan Nonsense Suppression in Yeast Cells Overproducing Sup35 (eRF3) Is Caused by Its Non-heritable Amyloids J. Biol. Chem., March 11, 2005; 280(10): 8808 - 8812. [Abstract] [Full Text] [PDF]

				K. D. Allen, R. D. Wegrzyn, T. A. Chernova, S. Muller, G. P. Newnam, P. A. Winslett, K. B. Wittich, K. D. Wilkinson, and Y. O. Chernoff Hsp70 Chaperones as Modulators of Prion Life Cycle: Novel Effects of Ssa and Ssb on the Saccharomyces cerevisiae Prion [PSI+] Genetics, March 1, 2005; 169(3): 1227 - 1242. [Abstract] [Full Text] [PDF]

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				S. Bagriantsev and S. W. Liebman Specificity of Prion Assembly in Vivo: [PSI+] AND [PIN+] FORM SEPARATE STRUCTURES IN YEAST J. Biol. Chem., December 3, 2004; 279(49): 51042 - 51048. [Abstract] [Full Text] [PDF]

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