[URE3] and [PSI] are prions of yeast and evidence for new fungal prions

Curr Issues Mol Biol. 2000 Apr;2(2):51-9.

Abstract

[URE3] and [PSI] are two non-Mendelian genetic elements discovered over 25 years ago and never assigned to a nucleic acid replicon. Their genetic properties led us to propose that they are prions, altered self-propagating forms of Ure2p and Sup35p, respectively, that cannot properly carry out the normal functions of these proteins. Ure2p is partially protease-resistant in [URE3] strains and Sup35p is aggregated specifically in [PSI] strains supporting this idea. Overexpression of Hsp104 cures [PSI], as does the absence of this protein, suggesting that the prion change of Sup35p in [PSI] strains is aggregation. Strains of [PSI], analogous to those described for scrapie, have now been described as well as an in vitro system for [PSI] propagation. Recently, two new potential prions have been described, one in yeast and the other in the filamentous fungus, Podospora.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Fungal Proteins / genetics
  • Genes, Fungal
  • Glutathione Peroxidase
  • Models, Genetic
  • Molecular Sequence Data
  • Mutation
  • Peptide Termination Factors
  • Phenotype
  • PrPSc Proteins / genetics
  • Prions / genetics*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • Sordariales / genetics

Substances

  • Fungal Proteins
  • Peptide Termination Factors
  • PrPSc Proteins
  • Prions
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Glutathione Peroxidase
  • URE2 protein, S cerevisiae