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Reference: Fernandez-Bellot E, et al. (2002) The [URE3] phenotype: evidence for a soluble prion in yeast. EMBO Rep 3(1):76-81

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Abstract

The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explaining the prion propagation of the phenotypes [PSI+] and [URE3], respectively. Here, we demonstrate that the propagation of [URE3] cannot simply be the consequence of generating large aggregates of Ure2p, because such aggregation can be found in some conditions that are not related to the prion state of Ure2p. A comparison of [PSI+] and [URE3] aggregation demonstrates differences between these two prion mechanisms. Our findings lead us to propose a new unifying model for yeast prion propagation.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Fernandez-Bellot E, Guillemet E, Ness F, Baudin-Baillieu A, Ripaud L, Tuite M, Cullin C
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