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. 1995 May 12;268(5212):880-4.
doi: 10.1126/science.7754373.

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

Y O Chernoff  1 , S L Lindquist, B Ono, S G Inge-Vechtomov, S W Liebman
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Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]

Y O Chernoff et al. Science. .

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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