Abstract:
:The yeast [PSI+] factor is inherited by a prion mechanism involving self-propagating Sup35p aggregates. We find that Sup35p prion function is conserved among distantly related yeasts. As with mammalian prions, a species barrier inhibits prion induction between Sup35p from different yeast species. This barrier is faithfully reproduced in vitro where, remarkably, ongoing polymerization of one Sup35p species does not affect conversion of another. Chimeric analysis identifies a short domain sufficient to allow foreign Sup35p to cross this barrier. These observations argue that the species barrier results from specificity in the growing aggregate, mediated by a well-defined epitope on the amyloid surface and, together with our identification of a novel yeast prion domain, show that multiple prion-based heritable states can propagate independently within one cell.
journal_name
Celljournal_title
Cellauthors
Santoso A,Chien P,Osherovich LZ,Weissman JSdoi
10.1016/s0092-8674(00)81565-2subject
Has Abstractpub_date
2000-01-21 00:00:00pages
277-88issue
2eissn
0092-8674issn
1097-4172pii
S0092-8674(00)81565-2journal_volume
100pub_type
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