Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+].
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.
Chernoff
Y O
YO
Department of Biological Sciences, University of Illinois, Chicago 60607-7020, USA.
Lindquist
S L
SL
Ono
B
B
Inge-Vechtomov
S G
SG
Liebman
S W
SW
D005656:Fungal Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000502:physiology; D015870:Gene Expression; D006360:Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D009154:Mutation; D011328:Prions / Q000096:biosynthesis*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins; D013489:Suppression, Genetic
D005656:Fungal Proteins; D006360:Heat-Shock Proteins; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae