The complexity and implications of yeast prion domains

被引:0
作者
Du, Zhiqiang [1 ]
机构
[1] Northwestern Univ, Dept Mol Pharmacol & Biol Chem, Chicago, IL 60611 USA
基金
美国国家卫生研究院;
关键词
yeast; Saccharomyces cerevisiae; prion; transcription; amyloid aggregates; prion domain; amino acid composition; Swi1; SACCHAROMYCES-CEREVISIAE; PSI+ PRION; AMYLOID FORMATION; BUDDING YEAST; HET-S; PROTEIN; PROPAGATION; AGGREGATION; DETERMINANT; SUP35;
D O I
10.4161/pri.5.4.18304
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:311 / 316
页数:6
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