title: Prion diseases of yeast: amyloid structure and biology.
abstract: Prion "variants" or "strains" are prions with the identical protein sequence, but different characteristics of the prion infection: e.g. different incubation periods for scrapie strains or different phenotype intensities for yeast prion variants. We have shown that infectious amyloids of the yeast prions [PSI+], [URE3] and [PIN+] each have an in-register parallel β-sheet architecture. Moreover, we have pointed out that this amyloid architecture can explain how one protein can faithfully transmit any of several conformations to new protein monomers. This explains how proteins can be genes.
authors.affiliation: Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0830, United States. wickner@helix.nih.gov
authors.forename: Reed B
authors.initials: RB
authors.lastname: Wickner
authors.forename: Herman K
authors.initials: HK
authors.lastname: Edskes
authors.forename: Dmitry
authors.initials: D
authors.lastname: Kryndushkin
authors.forename: Ryan
authors.initials: R
authors.lastname: McGlinchey
authors.forename: David
authors.initials: D
authors.lastname: Bateman
authors.forename: Amy
authors.initials: A
authors.lastname: Kelly
mesh_terms: D000682:Amyloid / Q000737:chemistry* / Q000235:genetics; D000818:Animals; D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism; D008961:Models, Structural; D017096:Prion Diseases / Q000378:metabolism*; D011328:Prions / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins