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

doi:10.1128/MCB.20.23.8916-8922.2000

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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-propagatingamyloidosis. We find that an insertion mutation or deletion ofHSP104 results in inability to propagate the [URE3] prion. Ourresults indicate that Hsp104 is a common factor in the maintenanceof two independent yeast prions. However, overproduction of Hsp104does not affect the stability of [URE3], in contrast to what isfound for the [PSI⁺] prion, which is known to be cured by either overproduction ordeficiency of Hsp104. Like Hsp104, the Hsp40 class chaperone Ydj1p,with the Hsp70 class Ssa1p, can renature proteins. We find thatoverproduction of Ydj1p results in a gradual complete loss of[URE3]. The involvement of protein chaperones in the propagationof [URE3] indicates a role for protein conformation ininheritance.

^* 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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