The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)]

Mol Microbiol. 2001 Jan;39(1):37-46. doi: 10.1046/j.1365-2958.2001.02224.x.


Overproduced fusions of Sup35 or its prion domain with green fluorescent protein (GFP) have previously been shown to form frequent dots in [PSI(+)] cells. Rare foci seen in [psi(-)] cells were hypothesized to indicate the de novo induction of [PSI(+)] caused by the overproduced prion domain. Here, we describe novel ring-type aggregates that also appear in [psi(-)] cultures upon Sup35 overproduction and show directly that dot and ring aggregates only appear in cells that have become [PSI(+)]. The formation of either type of aggregate requires [PIN(+)], an element needed for the induction of [PSI(+)]. Although aggregates are visible predominantly in stationary-phase cultures, [PSI(+)] induction starts in exponential phase, suggesting that much smaller aggregates can also propagate [PSI(+)]. Such small aggregates are probably present in [PSI(+)] cells and, upon Sup35-GFP overproduction, facilitate the frequent formation of dot aggregates, but only the occasional appearance of ring aggregates. In contrast, rings are very frequent when [PSI(+)] cultures, including those lacking [PIN(+)], are grown in the presence of GuHCl or excess Hsp104 while overexpressing Sup35-GFP. Thus, intermediates formed during [PSI(+)] curing seem to facilitate ring formation. Surprisingly, GuHCl and excess Hsp104, which are known to promote loss of [PSI(+)], did not prevent the de novo induction of [PSI(+)] by excess Sup35 in [psi(-)][PIN(+)] strains.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Fungal Proteins / biosynthesis*
  • Fungal Proteins / genetics
  • Green Fluorescent Proteins
  • Guanidine / pharmacology
  • Heat-Shock Proteins / biosynthesis
  • Luminescent Proteins / biosynthesis
  • Luminescent Proteins / genetics
  • Peptide Termination Factors
  • Prions / biosynthesis*
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / biosynthesis
  • Saccharomyces cerevisiae / drug effects
  • Saccharomyces cerevisiae / ultrastructure*
  • Saccharomyces cerevisiae Proteins*


  • Fungal Proteins
  • Heat-Shock Proteins
  • Luminescent Proteins
  • Peptide Termination Factors
  • Prions
  • Recombinant Fusion Proteins
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • HsP104 protein, S cerevisiae
  • Green Fluorescent Proteins
  • Guanidine