Propagation of the [PIN+] prion by fragments of Rnq1 fused to GFP

Curr Genet. 2007 May;51(5):309-19. doi: 10.1007/s00294-007-0127-0. Epub 2007 Apr 6.


Prions are viewed as enigmatic infectious entities whose genetic properties are enciphered solely in an array of self-propagating protein aggregate conformations. Rnq1, a yeast protein with yet unknown function, forms a prion named [PIN+] for its ability to facilitate the de novo induction of another prion, [PSI+]. Here we investigate a set of RNQ1 truncations that were designed to cover major Rnq1 sequence elements similar to those important for the propagation of other yeast prions: a region rich in asparagines and glutamines and several types of oligopeptide repeats. Proteins encoded by these RNQ1 truncations were tested for their ability to (a) join (decorate) pre-existing [PIN+] aggregates made of wild-type Rnq1 and (b) maintain the heritable aggregated state in the absence of wild-type RNQ1. While the possible involvement of particular sequence elements in the propagation of [PIN+] is discussed, the major result is that the efficiency of transmission of [PIN+] from wild-type Rnq1 to a fragment decreased with the fragment's length.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Alleles
  • Amino Acid Motifs
  • Amino Acid Sequence
  • Green Fluorescent Proteins / genetics*
  • Molecular Sequence Data
  • Prions / chemistry
  • Prions / genetics*
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics*


  • Prions
  • RNQ1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Green Fluorescent Proteins