Stress and prions: Lessons from the yeast model

Chernoff, Yury O.

doi:10.1016/j.febslet.2007.04.075

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Volume 581, Issue 19 , Pages 3695-3701, 31 July 2007

Stress and prions: Lessons from the yeast model

Edited by Robert Barouki

School of Biology and Institute for Bioengineering and Bioscience, Georgia Institute of Technology, Atlanta, GA 30332-0230, USA

Received 7 March 2007; received in revised form 20 April 2007; accepted 21 April 2007. published online 09 May 2007.

Abstract

Yeast self-perpetuating amyloids (prions) provide a convenient model for studying the cellular control of highly ordered aggregates involved in mammalian protein assembly disorders. The very ability of an amyloid to propagate a prion state in yeast is determined by its interactions with the stress-inducible chaperone Hsp104. Prion formation and propagation are also influenced by other stress-related chaperones (Hsp70 and Hsp40), and by alterations of the protein trafficking and degradation networks. Some stress conditions induce prion formation or loss. It is proposed that prions arise as byproducts of the reversible assembly of highly ordered complexes, protecting certain proteins during unfavorable conditions.

Keywords: Amyloid, Protein aggregation, Chaperone, Heat shock protein, Ubiquitin, Saccharomyces cerevisiae