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. 1996 Aug 2;273(5275):622-6.
doi: 10.1126/science.273.5275.622.

Support for the prion hypothesis for inheritance of a phenotypic trait in yeast

M M Patino  1 , J J Liu, J R Glover, S Lindquist
Affiliations

Support for the prion hypothesis for inheritance of a phenotypic trait in yeast

M M Patino et al. Science. .

Abstract

A cytoplasmically inherited genetic element in yeast, [PSI+], was confirmed to be a prionlike aggregate of the cellular protein Sup35 by differential centrifugation analysis and microscopic localization of a Sup35-green fluorescent protein fusion. Aggregation depended on the intracellular concentration and functional state of the chaperone protein Hsp104 in the same manner as did [PSI+] inheritance. The amino-terminal and carboxy-terminal domains of Sup35 contributed to the unusual behavior of [PSI+]. [PSI+] altered the conformational state of newly synthesized prion proteins, inducing them to aggregate as well, thus fulfilling a major tenet of the prion hypothesis.

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Comment in

  • Yeast prions: DNA-free genetics.
    Vogel G. Vogel G. Science. 1996 Aug 2;273(5275):580. doi: 10.1126/science.273.5275.580. Science. 1996. PMID: 8701310 No abstract available.

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