[URE3] and [PSI] are prions of yeast and evidence for new fungal prions.
[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.
Masison
D C
DC
National Institutes of Health, Bethesda, MD 20892-0830, USA.
Edskes
H K
HK
Maddelein
M L
ML
Taylor
K L
KL
Wickner
R B
RB
D000595:Amino Acid Sequence; D005656:Fungal Proteins / Q000235:genetics; D005800:Genes, Fungal; D005979:Glutathione Peroxidase; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009154:Mutation; D010454:Peptide Termination Factors; D010641:Phenotype; D018620:PrPSc Proteins / Q000235:genetics; D011328:Prions / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D020037:Sordariales / Q000235:genetics
D005656:Fungal Proteins; D010454:Peptide Termination Factors; D018620:PrPSc Proteins; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D005979:Glutathione Peroxidase; C067020:URE2 protein, S cerevisiae