Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved

Genetics. 2011 May;188(1):81-90. doi: 10.1534/genetics.111.127217. Epub 2011 Mar 2.

Abstract

[URE3] is a prion (infectious protein) of the Saccharomyces cerevisiae Ure2p, a regulator of nitrogen catabolism. We show that wild S. paradoxus can be infected with a [URE3] prion, supporting the use of S. cerevisiae as a prion test bed. We find that the Ure2p of Candida albicans and C. glabrata also regulate nitrogen catabolism. Conservation of amino acid sequence within the prion domain of Ure2p has been proposed as evidence that the [URE3] prion helps its host. We show that the C. albicans Ure2p, which does not conserve this sequence, can nonetheless form a [URE3] prion in S. cerevisiae, but the C. glabrata Ure2p, which does have the conserved sequence, cannot form [URE3] as judged by its performance in S. cerevisiae. These results suggest that the sequence is not conserved to preserve prion forming ability.

Publication types

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

MeSH terms

  • Candida / drug effects
  • Candida / genetics
  • Candida / metabolism
  • Conserved Sequence / genetics*
  • Evolution, Molecular*
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Gene Expression Regulation, Fungal / drug effects
  • Genes, Fungal / genetics
  • Green Fluorescent Proteins / metabolism
  • Guanidine / pharmacology
  • Nitrogen / metabolism
  • Prions / chemistry
  • Prions / metabolism*
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Saccharomyces / drug effects
  • Saccharomyces / genetics
  • Saccharomyces / metabolism
  • Species Specificity
  • Terminology as Topic
  • Yeasts / drug effects
  • Yeasts / genetics
  • Yeasts / growth & development
  • Yeasts / metabolism*

Substances

  • Fungal Proteins
  • Prions
  • Green Fluorescent Proteins
  • Guanidine
  • Nitrogen