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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Fungal Proteins / analysis
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Fungal Proteins / chemistry*
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Fungal Proteins / genetics
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Fungal Proteins / physiology
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Green Fluorescent Proteins
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Heat-Shock Proteins / physiology
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Luminescent Proteins / analysis
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Molecular Sequence Data
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Peptide Termination Factors
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Phenotype
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Prions / chemistry*
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Prions / genetics
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Protein Conformation*
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Recombinant Fusion Proteins / analysis
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Recombinant Fusion Proteins / chemistry
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Saccharomyces cerevisiae / chemistry*
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae Proteins*
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Solubility
Substances
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Fungal Proteins
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Heat-Shock Proteins
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Luminescent Proteins
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Peptide Termination Factors
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Prions
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Recombinant Fusion Proteins
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SUP35 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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HsP104 protein, S cerevisiae
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Green Fluorescent Proteins