The [URE3] phenotype:: evidence for a soluble prion in yeast

被引：24

作者：

Fernandez-Bellot, E

Guillemet, E

Ness, F

Baudin-Baillieu, A

Ripaud, L

Tuite, M

Cullin, C

机构：

[1] Inst Biochim & Genet Cellulaires, F-33077 Bordeaux, France

[2] Ctr Genet Mol, F-91190 Gif Sur Yvette, France

[3] Univ Kent, Dept Biosci, Canterbury CT2 7NJ, Kent, England

来源：

EMBO REPORTS | 2002年 / 3卷 / 01期

关键词：

D O I：

10.1093/embo-reports/kvf011

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

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页码：76 / 81

页数：6

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