Science · 1995 · 1K citations · 28 references
The yeast prion-like factor ψ+ is a self-modified protein analogous to mammalian prions. The study aims to explore chaperone modulation as a potential antiprion therapy. An optimal intermediate level of Hsp104 is required for ψ+ propagation; both overproduction and loss of Hsp104 eliminate ψ+, indicating that precise chaperone levels can cure cells of prions without harming viability.
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. Overproduction 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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Mice devoid of PrP are resistant to scrapie
Hansruedi Büeler, Adriano Aguzzi, Andreas W. Sailer et al. · Cell · 1993 · 2.1K citations · Full text
Protein disaggregation mediated by heat-shock protein Hspl04
Dawn A. Parsell, Anthony S. Kowal, Mike A. Singer et al. · Nature · 1994 · 869 citations
HSP104 Required for Induced Thermotolerance
Yolanda Sánchez, Susan Lindquist · Science · 1990 · 851 citations
Hsp104 is required for tolerance to many forms of stress.
Yolanda Sánchez, J Taulien, Katherine A. Borkovich et al. · The EMBO Journal · 1992 · 580 citations · Full text
Psychiatry, Stress, Many Forms +5