Support for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast

作者：María M. Patiño, Jiajia Liu, John R. Glover, Susan Lee Lindquist · 发表于：Science · 年份：1996 · DOI：10.1126/science.273.5275.622 · 被引用次数：619 · 研究领域：Prion Diseases and Protein Misfolding、Trace Elements in Health、Neurological diseases and metabolism

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.