title: Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.
abstract: Sup35p of Saccharomyces cerevisiae can form the [PSI+] prion, an infectious amyloid in which the protein is largely inactive. The part of Sup35p that forms the amyloid is the region normally involved in control of mRNA turnover. The formation of [PSI+] by Sup35p's from other yeasts has been interpreted to imply that the prion-forming ability of Sup35p is conserved in evolution, and thus of survival/fitness/evolutionary value to these organisms. We surveyed a larger number of yeast and fungal species by the same criteria as used previously and find that the Sup35p from many species cannot form prions. [PSI+] could be formed by the Sup35p from Candida albicans, Candida maltosa, Debaromyces hansenii, and Kluyveromyces lactis, but orders of magnitude less often than the S. cerevisiae Sup35p converts to the prion form. The Sup35s from Schizosaccharomyces pombe and Ashbya gossypii clearly do not form [PSI+]. We were also unable to detect [PSI+] formation by the Sup35ps from Aspergillus nidulans, Aspergillus fumigatus, Magnaporthe grisea, Ustilago maydis, or Cryptococcus neoformans. Each of two C. albicans SUP35 alleles can form [PSI+], but transmission from one to the other is partially blocked. These results suggest that the prion-forming ability of Sup35p is not a conserved trait, but is an occasional deleterious side effect of a protein domain conserved for another function.
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830 hermane@helix.nih.gov.
authors: Herman K
authors: HK
authors: Edskes
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Hima J
authors: HJ
authors: Khamar
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Chia-Lin
authors: CL
authors: Winchester
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Alexandria J
authors: AJ
authors: Greenler
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Albert
authors: A
authors: Zhou
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Ryan P
authors: RP
authors: McGlinchey
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Anton
authors: A
authors: Gorkovskiy
authors: Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830.
authors: Reed B
authors: RB
authors: Wickner
mesh_terms: D000682:Amyloid / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D010454:Peptide Termination Factors / Q000737:chemistry*; D010802:Phylogeny; D011328:Prions / Q000737:chemistry*; D066329:Protein Aggregates; D017510:Protein Folding; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; D010454:Peptide Termination Factors; D011328:Prions; D066329:Protein Aggregates; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C459790:Sup35 protein, Candida albicans
keywords: Ashbya gossypii; Schizosaccharomyces pombe; [PSI+] prion; cytoduction