Similar and divergent features in mammalian and yeast prions

被引：14

作者：

Bousset, L ^{[1
]}

Melki, R ^{[1
]}

机构：

[1] CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France

来源：

MICROBES AND INFECTION | 2002年 / 4卷 / 04期

关键词：

prion; amyloid fibrils; PrP; SuP35p; Ure2p; Saccharomyces cerevisiae; auto-assembly; nucleation-polymerization; structural inheritance; conformational changes; molecular chaperones;

D O I：

10.1016/S1286-4579(02)01561-7

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Mammalian transmissible spongiform encephalopathies are likely due to the propagation of an abnormal form of a constitutive protein instead of traditional genetic material (nucleic acids). Such infectious proteins, which are termed prions, exist in yeast. They are at the origin of a number of phenotypes that are inherited in a non-Mendelian manner. These prions are very useful to dissect the molecular events at the origin of this structure-based inheritance. The properties of mammalian and yeast prions are presented and compared. This review highlights a number of similarities and differences. (C) 2002 Editions scientifiques et medicales Elsevier SAS. All rights reserved.

引用

页码：461 / 469

页数：9

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