The [URE3] phenotype: evidence for a soluble prion in yeast.
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.
Fernandez-Bellot
Eric
E
Centre de Génétique Moléculaire, 91190 Gif-sur-Yvette, France.
Guillemet
Elisabeth
E
Ness
Frederique
F
Baudin-Baillieu
Agnes
A
Ripaud
Leslie
L
Tuite
Mick
M
Cullin
Christophe
C
D000595:Amino Acid Sequence; D005979:Glutathione Peroxidase; D008969:Molecular Sequence Data; D010641:Phenotype; D011328:Prions / Q000737:chemistry* / Q000235:genetics; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics; D012995:Solubility
D011328:Prions; D020033:Protein Isoforms; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; D005979:Glutathione Peroxidase; C067020:URE2 protein, S cerevisiae