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Viruses 2019, 11(4), 349; https://doi.org/10.3390/v11040349

Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast

Department of Chemistry, Lafayette College, Easton, PA 18042, USA
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Author to whom correspondence should be addressed.
Received: 15 March 2019 / Revised: 12 April 2019 / Accepted: 14 April 2019 / Published: 16 April 2019
(This article belongs to the Special Issue Deciphering the Molecular Targets of Prion and Prion-Like Strains)
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Abstract

Yeast prions are protein-based genetic elements found in the baker’s yeast Saccharomyces cerevisiae, most of which are amyloid aggregates that propagate by fragmentation and spreading of small, self-templating pieces called propagons. Fragmentation is carried out by molecular chaperones, specifically Hsp104, Hsp70, and Hsp40. Like other amyloid-forming proteins, amyloid-based yeast prions exhibit structural polymorphisms, termed “strains” in mammalian systems and “variants” in yeast, which demonstrate diverse phenotypes and chaperone requirements for propagation. Here, the known differential interactions between chaperone proteins and yeast prion variants are reviewed, specifically those of the yeast prions [PSI+], [RNQ+]/[PIN+], and [URE3]. For these prions, differences in variant-chaperone interactions (where known) with Hsp104, Hsp70s, Hsp40s, Sse1, and Hsp90 are summarized, as well as some interactions with chaperones of other species expressed in yeast. As amyloid structural differences greatly impact chaperone interactions, understanding and accounting for these variations may be crucial to the study of chaperones and both prion and non-prion amyloids. View Full-Text
Keywords: Ssa; Ssb; Ydj1; Apj1; Swa2; Sis1; J-protein; Hdj1 Ssa; Ssb; Ydj1; Apj1; Swa2; Sis1; J-protein; Hdj1
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Killian, A.N.; Miller, S.C.; Hines, J.K. Impact of Amyloid Polymorphism on Prion-Chaperone Interactions in Yeast. Viruses 2019, 11, 349.

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