title: Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.
abstract: Yeast prions (infectious proteins) were discovered by their outré genetic properties and have become important models for an array of human prion and amyloid diseases. A single prion protein can become any of many distinct amyloid forms (called prion variants or strains), each of which is self-propagating, but with different biological properties (eg, lethal vs mild). The folded in-register parallel β sheet architecture of the yeast prion amyloids naturally suggests a mechanism by which prion variant information can be faithfully transmitted for many generations. The yeast prions rely on cellular chaperones for their propagation, but can be cured by various chaperone imbalances. The Btn2/Cur1 system normally cures most variants of the [URE3] prion that arise. Although most variants of the [PSI+] and [URE3] prions are toxic or lethal, some are mild in their effects. Even the most mild forms of these prions are rare in the wild, indicating that they too are detrimental to yeast. The beneficial [Het-s] prion of Podospora anserina poses an important contrast in its structure, biology, and evolution to the yeast prions characterized thus far.
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
authors.forename: R B
authors.initials: RB
authors.lastname: Wickner
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
authors.forename: H K
authors.initials: HK
authors.lastname: Edskes
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
authors.forename: A
authors.initials: A
authors.lastname: Gorkovskiy
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
authors.forename: E E
authors.initials: EE
authors.lastname: Bezsonov
authors.affiliation: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, United States.
authors.forename: E E
authors.initials: EE
authors.lastname: Stroobant
mesh_terms: D000595:Amino Acid Sequence; D000682:Amyloid / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000686:Amyloidosis / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008956:Models, Chemical; D018832:Molecular Chaperones / Q000378:metabolism; D008969:Molecular Sequence Data; D017096:Prion Diseases / Q000378:metabolism* / Q000635:transmission; D011328:Prions / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D015003:Yeasts / Q000235:genetics / Q000378:metabolism*
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; D018832:Molecular Chaperones; D011328:Prions
keywords: Antiprion system; Btn2; Chaperone; Protein gene; Sup35; Ure2; [Het-s]; [PSI+]; [URE3]