Rnq1: An Epigenetic Modifier of Protein Function in Yeast

Mol Cell. 2000 Jan;5(1):163-72. doi: 10.1016/s1097-2765(00)80412-8.

Abstract

Two protein-based genetic elements (prions) have been identified in yeast. It is not clear whether other prions exist, nor is it understood how one might find them. We established criteria for searching protein databases for prion candidates and found several. The first examined, Rnq1, exists in distinct, heritable physical states, soluble and insoluble. The insoluble state is dominant and transmitted between cells through the cytoplasm. When the prion-like region of Rnq1 was substituted for the prion domain of Sup35, the protein determinant of the prion [PSI+], the phenotypic and epigenetic behavior of [PSI+] was fully recapitulated. These findings identity Rnq1 as a prion, demonstrate that prion domains are modular and transferable, and establish a paradigm for identifying and characterizing novel prions.

Publication types

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

MeSH terms

  • Cloning, Molecular
  • Crosses, Genetic
  • Fungal Proteins / chemistry
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Deletion
  • Open Reading Frames
  • Peptide Termination Factors
  • Phenotype
  • Polymerase Chain Reaction
  • Prions / chemistry
  • Prions / genetics*
  • Prions / metabolism*
  • Promoter Regions, Genetic
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae Proteins*
  • Suppression, Genetic

Substances

  • Fungal Proteins
  • Peptide Termination Factors
  • Prions
  • RNQ1 protein, S cerevisiae
  • Recombinant Fusion Proteins
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins