Insights into the Nature of Yeast Prions

Osherovich, Lev; Weissman, Jonathan S.

doi:10.1002/9783527619498.ch68

Cited by 1 publication

(2 citation statements)

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“…Prion inheritance requires three sequential events that must keep pace with cell division to preserve the number of heritable prion units, or propagons, per cell (Osherovich and Weissman 2004). First, prion aggregates must grow in size by incorporating newly synthesized protein.…”

Section: Discussionmentioning

confidence: 99%

“…Prions are a special class of protein aggregates that replicate their conformation and spread infectiously (Prusiner 1998). After the discovery that prion aggregates are responsible for the mammalian transmissible spongiform encephalopathies, several epigenetically heritable traits in fungi were also found to depend on a prion mechanism (Wickner 1994; Uptain and Lindquist 2002; Osherovich and Weissman 2004). In Saccharomyces cerevisiae and Podospora anserina, prions are transmitted from cell to cell through mating and cell division, resulting in readily assayed phenotypes with a non-Mendelian pattern of inheritance (Liebman and Derkatch 1999).…”

Section: Introductionmentioning

confidence: 99%

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Dissection and Design of Yeast Prions

et al. 2004

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Many proteins can misfold into β-sheet-rich, self-seeding polymers (amyloids). Prions are exceptional among such aggregates in that they are also infectious. In fungi, prions are not pathogenic but rather act as epigenetic regulators of cell physiology, providing a powerful model for studying the mechanism of prion replication. We used prion-forming domains from two budding yeast proteins (Sup35p and New1p) to examine the requirements for prion formation and inheritance. In both proteins, a glutamine/asparagine-rich (Q/N-rich) tract mediates sequence-specific aggregation, while an adjacent motif, the oligopeptide repeat, is required for the replication and stable inheritance of these aggregates. Our findings help to explain why although Q/N-rich proteins are relatively common, few form heritable aggregates: prion inheritance requires both an aggregation sequence responsible for self-seeded growth and an element that permits chaperone-dependent replication of the aggregate. Using this knowledge, we have designed novel artificial prions by fusing the replication element of Sup35p to aggregation-prone sequences from other proteins, including pathogenically expanded polyglutamine.

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Section: Discussionmentioning

confidence: 99%