title: Prions are affected by evolution at two levels.
abstract: Prions, infectious proteins, can transmit diseases or be the basis of heritable traits (or both), mostly based on amyloid forms of the prion protein. A single protein sequence can be the basis for many prion strains/variants, with different biological properties based on different amyloid conformations, each rather stably propagating. Prions are unique in that evolution and selection work at both the level of the chromosomal gene encoding the protein, and on the prion itself selecting prion variants. Here, we summarize what is known about the evolution of prion proteins, both the genes and the prions themselves. We contrast the one known functional prion, [Het-s] of Podospora anserina, with the known disease prions, the yeast prions [PSI+] and [URE3] and the transmissible spongiform encephalopathies of mammals.
authors.affiliation: Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bldg. 8, Room 225, 8 Center Drive MSC 0830, Bethesda, MD, 20892-0830, USA. wickner@helix.nih.gov.
authors.forename: Reed B
authors.initials: RB
authors.lastname: Wickner
authors.affiliation: Laboratory of Biochemistry and Genetics, National Institute of Diabetes Digestive and Kidney Diseases, National Institutes of Health, Bldg. 8, Room 225, 8 Center Drive MSC 0830, Bethesda, MD, 20892-0830, USA. amy.kelly@ars.usda.gov.|NCAUR, Agricultural Research Service, U.S. Department of Agriculture, 1815 N. University St., Peoria, IL, 61604, USA. amy.kelly@ars.usda.gov.
authors.forename: Amy C
authors.initials: AC
authors.lastname: Kelly
mesh_terms: D000682:Amyloid / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D019143:Evolution, Molecular; D005656:Fungal Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D005979:Glutathione Peroxidase / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D006801:Humans; D010454:Peptide Termination Factors / Q000032:analysis / Q000235:genetics / Q000378:metabolism; D048468:Podospora / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017096:Prion Diseases / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D011328:Prions / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000032:analysis / Q000235:genetics / Q000378:metabolism
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; C083891:HET-S protein, Podospora anserina; D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D005979:Glutathione Peroxidase; C067020:URE2 protein, S cerevisiae
keywords: Amyloid; HET-s; Parallel in-register beta sheet; Rnq1; Sup35p; Ure2p