title: The complexity and implications of yeast prion domains.
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.
authors.affiliation: Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, IL, USA. z-du@northwestern.edu
authors.forename: Zhiqiang
authors.initials: Z
authors.lastname: Du
mesh_terms: D001216:Asparagine / Q000737:chemistry; D005973:Glutamine / Q000737:chemistry; D011328:Prions / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry
chemical_list: D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D005973:Glutamine; D001216:Asparagine