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Prion. 2011 Oct-Dec;5(4):258-62. doi: 10.4161/pri.17748. Epub 2011 Oct 1.

The yeast prions [PSI+] and [URE3] are molecular degenerative diseases.

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1
Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Disease, National Institutes of Health, Bethesda, MD, USA. wickner@helix.nih.gov

Abstract

The yeast prions [URE3] and [PSI] are not found in wild strains, suggesting they are not an advantage. Prion-forming ability is not conserved, even within Saccharomyces, suggesting it is a disease. Prion domains have non-prion functions, explaining some conservation of sequence. However, in spite of the sequence being constrained in evolution by these non-prion functions, the prion domains vary more rapidly than the remainder of the molecule, and these changes produce a transmission barrier, suggesting that these changes were selected to block prion infection. Yeast prions [PSI] and [URE3] induce a cellular stress response (Hsp104 and Hsp70 induction), suggesting the cells are not happy about being infected. Recently, we showed that the array of [PSI] and [URE3] prions includes a majority of lethal or very toxic variants, a result not expected if either prion were an adaptive cellular response to stress.

PMID:
22052353
PMCID:
PMC4012404
DOI:
10.4161/pri.17748
[Indexed for MEDLINE]
Free PMC Article
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