Literature DB >> 7754373

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

Y O Chernoff1, S L Lindquist, B Ono, S G Inge-Vechtomov, S W Liebman.   

Abstract

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 certain level of chaperone expression can cure cells of prions without affecting viability. This may lead to antiprion treatments that involve the alteration of chaperone amounts or activity.

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Year:  1995        PMID: 7754373     DOI: 10.1126/science.7754373

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  502 in total

1.  Mutational analysis of the [Het-s] prion analog of Podospora anserina. A short N-terminal peptide allows prion propagation.

Authors:  V Coustou; C Deleu; S J Saupe; J Bégueret
Journal:  Genetics       Date:  1999-12       Impact factor: 4.562

2.  Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion.

Authors:  Y O Chernoff; G P Newnam; J Kumar; K Allen; A D Zink
Journal:  Mol Cell Biol       Date:  1999-12       Impact factor: 4.272

3.  Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network.

Authors:  P Goloubinoff; A Mogk; A P Zvi; T Tomoyasu; B Bukau
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-23       Impact factor: 11.205

4.  Conformational propagation with prion-like characteristics in a simple model of protein folding.

Authors:  P M Harrison; H S Chan; S B Prusiner; F E Cohen
Journal:  Protein Sci       Date:  2001-04       Impact factor: 6.725

5.  Dependence and independence of [PSI(+)] and [PIN(+)]: a two-prion system in yeast?

Authors:  I L Derkatch; M E Bradley; S V Masse; S P Zadorsky; G V Polozkov; S G Inge-Vechtomov; S W Liebman
Journal:  EMBO J       Date:  2000-05-02       Impact factor: 11.598

6.  Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation.

Authors:  K Doh-Ura; T Iwaki; B Caughey
Journal:  J Virol       Date:  2000-05       Impact factor: 5.103

7.  Strains of [PSI(+)] are distinguished by their efficiencies of prion-mediated conformational conversion.

Authors:  S M Uptain; G J Sawicki; B Caughey; S Lindquist
Journal:  EMBO J       Date:  2001-11-15       Impact factor: 11.598

8.  Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  EMBO J       Date:  2002-01-15       Impact factor: 11.598

9.  The [URE3] phenotype: evidence for a soluble prion in yeast.

Authors:  Eric Fernandez-Bellot; Elisabeth Guillemet; Frederique Ness; Agnes Baudin-Baillieu; Leslie Ripaud; Mick Tuite; Christophe Cullin
Journal:  EMBO Rep       Date:  2001-12-19       Impact factor: 8.807

10.  Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  2002-02-26       Impact factor: 11.205

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