The complexity and implications of yeast prion domains

Zhiqiang Du*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

26 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)311-316
Number of pages6
JournalPrion
Volume5
Issue number4
DOIs
StatePublished - Oct 2011

Keywords

  • Amino acid composition
  • Amyloid aggregates
  • Prion
  • Prion domain
  • Saccharomyces cerevisiae
  • Swi1
  • Transcription
  • Yeast

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience
  • Cell Biology
  • Infectious Diseases

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