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

Patino, Maria M., Liu, Jia-Jia, Glover, John R., Lindquist, Susan·1996·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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Metadata

Authors
Patino, M. M., Liu, J.-J., Glover, J. R., & Lindquist, S.
Venue
Science
Published
1996-08-02
Volume
273
Issue
5275
Pages
622-626
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1989172027
Cited by
611
References
0
FWCI
9.15
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Support for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast. https://app.cochat.ai/papers/10.1126/science.273.5275.622
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Patino, M. M., Liu, J.-J., Glover, J. R., & Lindquist, S. (1996). Support for the Prion Hypothesis for Inheritance of a Phenotypic Trait in Yeast. Science. https://doi.org/10.1126/science.273.5275.622

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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