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Article

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].

Science (New York, N.Y.) - 12 May 1995

Chernoff Y O, Lindquist S L, Ono B, Inge-Vechtomov S G, Liebman S W

Abstract excerpt

The yeast non-Mendelian factor [psi+] has been suggested to be a self-modified protein analogous to mammalian prions. Here it is reported that an intermediate amount of the chaperone protein Hsp104 was required for the propagation of the [psi+] factor. Over-production or inactivation of Hsp104 caused the loss of [psi+]. These results suggest that chaperone proteins play a role in prion-like phenomena, and that a...

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Identifiers

PMID: 7754373
DOI: 10.1126/science.7754373

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].PMID 7754373Read ↗

Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor.Semantic proximity Read ↗

Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae.Semantic proximity Read ↗

Support for the prion hypothesis for inheritance of a phenotypic trait in yeast.Semantic proximity Read ↗

Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model.Semantic proximity Read ↗

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers.Semantic proximity Read ↗

The [PSI+] prion of yeast: a problem of inheritance.Semantic proximity Read ↗

Importance of the Hsp70 ATPase domain in yeast prion propagation.Semantic proximity Read ↗

N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression.Semantic proximity Read ↗

A systematic evaluation of the function of the protein-remodeling factor Hsp104 in [PSI+] prion propagation in S. cerevisiae by comprehensive chromosomal mutations.Semantic proximity Read ↗

Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity.Semantic proximity Read ↗

Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation.Semantic proximity Read ↗

Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion.Semantic proximity Read ↗

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