A complete catalog of wild-type Sup35 prion variants and their protein-only propagation

被引:9
作者
Huang, Yu-Wen [1 ,2 ,3 ]
King, Chih-Yen [3 ]
机构
[1] Acad Sinica, Taiwan Int Grad Program, Mol & Cell Biol, Taipei, Taiwan
[2] Natl Def Med Ctr, Taipei, Taiwan
[3] Acad Sinica, Inst Mol Biol, Taipei 11529, Taiwan
关键词
PSI+; Prion; Variants; Amyloid; Saccharomyces cerevisiae; ATOMIC-RESOLUTION STRUCTURE; NON-MENDELIAN FACTOR; AMYLOID FIBRILS; INFECTIOUS CONFORMATION; STRUCTURAL BASIS; GENE DISRUPTION; CRYO-EM; YEAST; STRAIN; PSI+;
D O I
10.1007/s00294-019-01003-8
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
Twenty-three prion variants of the wild-type Sup35 protein are obtained, including 19 novel ones and 4 previously documented, namely, VH, VK, VL, and W8. Their uniqueness and non-composite nature are demonstrated. Specific infectivity is generated de novo for most variants by adding prion particles to solutions of a purified Sup35 N-terminal fragment, thereby supporting the protein-only composition. Sup35 prions isolated by other laboratories are identified within the collection and found to fall into a narrow set of five variant types that are readily inducible in vivo by Sup35 overexpression. The work establishes an unambiguous and extensive collection of prion variants, demonstrating that a protein, by itself, in the absence of genetic and conformational co-factors, could adopt a great number of structures. In light of recent high-resolution structures of other amyloids, we discuss how the diverse folding is achieved in spite of apparent contradiction to the classical paradigm that a protein's structure is uniquely determined by its sequence.
引用
收藏
页码:97 / 122
页数:26
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