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.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Fernandez-Bellot E,Guillemet E,Ness F,Baudin-Baillieu A,Ripaud L,Tuite M,Cullin Cdoi
10.1093/embo-reports/kvf011keywords:
subject
Has Abstractpub_date
2002-01-01 00:00:00pages
76-81issue
1eissn
1469-221Xissn
1469-3178pii
kvf011journal_volume
3pub_type
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