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

共 110 条

[1] GENETIC ASPECTS OF [URE3], A NON-MITOCHONDRIAL, CYTOPLASMICALLY INHERITED MUTATION IN YEAST [J].

AIGLE, M ;

LACROUTE, F .

MOLECULAR & GENERAL GENETICS, 1975, 136 (04) :327-335

[2] DOES AGENT OF SCRAPIE REPLICATE WITHOUT NUCLEIC ACID [J].

ALPER, T ;

CRAMP, WA ;

HAIG, DA ;

CLARKE, MC .

NATURE, 1967, 214 (5090) :764-&

[3] Identification of the Cu2+ binding sites in the N-terminal domain of the prion protein by EPR and CD spectroscopy [J].

Aronoff-Spencer, E ;

Burns, CS ;

Avdievich, NI ;

Gerfen, GJ ;

Peisach, J ;

Antholine, WE ;

Ball, HL ;

Cohen, FE ;

Prusiner, SB ;

Millhauser, GL .

BIOCHEMISTRY, 2000, 39 (45) :13760-13771

[4] An amyloid-forming peptide from the yeast prion Sup35 reveals a dehydrated β-sheet structure for amyloid [J].

Balbirnie, M ;

Grothe, R ;

Eisenberg, DS .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (05) :2375-2380

[5] PRION PROTEIN ISOFORMS, A CONVERGENCE OF BIOLOGICAL AND STRUCTURAL INVESTIGATIONS [J].

BALDWIN, MA ;

COHEN, FE ;

PRUSINER, SB .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (33) :19197-19200

[6] NONGENETIC PROPAGATION OF STRAIN-SPECIFIC PROPERTIES OF SCRAPIE PRION PROTEIN [J].

BESSEN, RA ;

KOCISKO, DA ;

RAYMOND, GJ ;

NANDAN, S ;

LANSBURY, PT ;

CAUGHEY, B .

NATURE, 1995, 375 (6533) :698-700

[7] IDENTIFICATION OF A PROTEIN THAT PURIFIES WITH THE SCRAPIE PRION [J].

BOLTON, DC ;

MCKINLEY, MP ;

PRUSINER, SB .

SCIENCE, 1982, 218 (4579) :1309-1311

[8] Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms [J].

Bossers, A ;

Belt, PBGM ;

Raymond, GJ ;

Caughey, B ;

deVries, R ;

Smits, MA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (10) :4931-4936

[9] Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds [J].

Bousset, L ;

Belrhali, H ;

Melki, R ;

Morera, S .

BIOCHEMISTRY, 2001, 40 (45) :13564-13573

[10] Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae [J].

Bousset, L ;

Belrhali, H ;

Janin, J ;

Melki, R ;

Morera, S .

STRUCTURE, 2001, 9 (01) :39-46

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