The complexity and implications of yeast prion domains

Prion. Oct-Dec 2011;5(4):311-6. doi: 10.4161/pri.18304. Epub 2011 Oct 1.

Abstract

Prions are infectious proteins with altered conformations converted from otherwise normal host proteins. While there is only one known mammalian prion protein, PrP, a handful of prion proteins have been identified in the yeast Saccharomyces cerevisiae. Yeast prion proteins usually have a defined region called prion domain (PrD) essential for prion properties, which are typically rich in glutamine (Q) and asparagine (N). Despite sharing several common features, individual yeast PrDs are generally intricate and divergent in their compositional characteristics, which potentially implicates their prion phenotypes, such as prion-mediated transcriptional regulations.

Publication types

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

MeSH terms

  • Asparagine / chemistry
  • Glutamine / chemistry
  • Prions / chemistry*
  • Prions / metabolism*
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transcription Factors / chemistry

Substances

  • Prions
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Glutamine
  • Asparagine