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

The complexity and implications of yeast prion domains.

Author information

1
Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, IL, USA. z-du@northwestern.edu

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.

PMID:
22156731
PMCID:
PMC4012399
DOI:
10.4161/pri.18304
[Indexed for MEDLINE]
Free PMC Article

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