Molecular basis of a yeast prion species barrier.

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

Cell

journal_title

Cell

authors

Santoso A,Chien P,Osherovich LZ,Weissman JS

doi

10.1016/s0092-8674(00)81565-2

subject

Has Abstract

pub_date

2000-01-21 00:00:00

pages

277-88

issue

2

eissn

0092-8674

issn

1097-4172

pii

S0092-8674(00)81565-2

journal_volume

100

pub_type

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