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Molecular and Cellular Biology, December 2000, p. 8916-8922, Vol. 20, No. 23
0270-7306/00/$04.00+0

[URE3] Prion Propagation in Saccharomyces cerevisiae: Requirement for Chaperone Hsp104 and Curing by Overexpressed Chaperone Ydj1p

Hiromitsu Moriyama, Herman K. Edskes, and Reed B. Wickner*

Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830

Received 3 July 2000/Returned for modification 29 August 2000/Accepted 11 September 2000

The [URE3] nonchromosomal genetic element is an infectious form (prion) of the Ure2 protein, apparently a self-propagating amyloidosis. We find that an insertion mutation or deletion of HSP104 results in inability to propagate the [URE3] prion. Our results indicate that Hsp104 is a common factor in the maintenance of two independent yeast prions. However, overproduction of Hsp104 does not affect the stability of [URE3], in contrast to what is found for the [PSI+] prion, which is known to be cured by either overproduction or deficiency of Hsp104. Like Hsp104, the Hsp40 class chaperone Ydj1p, with the Hsp70 class Ssa1p, can renature proteins. We find that overproduction of Ydj1p results in a gradual complete loss of [URE3]. The involvement of protein chaperones in the propagation of [URE3] indicates a role for protein conformation in inheritance.

* Corresponding author. Mailing address: Bldg. 8, Room 225, N.I.H., 8 Center Dr. MSC0830, Bethesda, MD 20892-0830. Phone: (301) 496-3452. Fax: (301) 402-0240. E-mail: wickner{at}helix.nih.gov.

Molecular and Cellular Biology, December 2000, p. 8916-8922, Vol. 20, No. 23
0270-7306/00/$04.00+0


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