Stress and prions: Lessons from the yeast model

被引：67

作者：

Chernoff, Yury O. ^{[1
]}

机构：

[1] Georgia Inst Technol, Sch Biol, Atlanta, GA 30332 USA

[2] Georgia Inst Technol, Inst Bioengn & Biosci, Atlanta, GA 30332 USA

来源：

FEBS LETTERS | 2007年 / 581卷 / 19期

关键词：

amyloid; protein aggregation; chaperone; heat shock protein; ubiquitin; Saccharomyces cerevisiae; UBIQUITIN-PROTEASOME SYSTEM; SACCHAROMYCES-CEREVISIAE; HEAT-SHOCK; HSP104; CHAPERONE; AGGREGATION; PROPAGATION; PROTEINS; DISEASE; PSI+;

D O I：

10.1016/j.febslet.2007.04.075

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：

Yeast self-perpetuating amyloids (prions) provide a convenient model for studying the cellular control of highly ordered aggregates involved in mammalian protein assembly disorders. The very ability of an amyloid to propagate a prion state in yeast is determined by its interactions with the stress-inducible chaperone Hsp104. Prion formation and propagation are also influenced by other stress-related chaperones (Hsp70 and Hsp40), and by alterations of the protein trafficking and degradation networks. Some stress conditions induce prion formation or loss. It is proposed that prions arise as byproducts of the reversible assembly of highly ordered complexes, protecting certain proteins during unfavorable conditions. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：3695 / 3701

页数：7

共 50 条

[1] Hsp70 chaperones as modulators of prion life cycle:: Novel effects of Ssa and Ssb on the Sacharomyces cerevisiae prion [PSI+] [J].

Allen, KD ;

Wegrzyn, RD ;

Chernova, TA ;

Müller, S ;

Newnam, GP ;

Winslett, PA ;

Wittich, KB ;

Wilkinson, KD ;

Chernoff, YO .

GENETICS, 2005, 169 (03) :1227-1242

[2] Effects of ubiquitin system alterations on the formation and loss of a yeast prion [J].

Allen, Kim D. ;

Chernova, Tatiana A. ;

Tennant, E. Paula ;

Wilkinson, Keith D. ;

Chernoff, Yury O. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (05) :3004-3013

[3] Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation [J].

Bennett, EJ ;

Bence, NF ;

Jayakumar, R ;

Kopito, RR .

MOLECULAR CELL, 2005, 17 (03) :351-365

[4] Prion variant maintained only at high levels of the Hsp104 disaggregase [J].

Borchsenius, AS ;

Müller, S ;

Newnam, GP ;

Inge-Vechtomov, SG ;

Chernoff, YO .

CURRENT GENETICS, 2006, 49 (01) :21-29

[5] Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds' [J].

Borchsenius, AS ;

Wegrzyn, RD ;

Newnam, GP ;

Inge-Vechtomov, SG ;

Chernoff, YO .

EMBO JOURNAL, 2001, 20 (23) :6683-6691

[6]

Brignull HR, 2007, ADV EXP MED BIOL, V594, P167

[7] Mechanisms of chaperone suppression of polyglutamine disease:: selectivity, synergy and medullation of protein solubility in Drosophila [J].

Chan, HYE ;

Warrick, JM ;

Gray-Board, GL ;

Paulson, HL ;

Bonini, NM .

HUMAN MOLECULAR GENETICS, 2000, 9 (19) :2811-2820

[8] Prion species barrier between the closely related yeast proteins is detected despite coaggregation [J].

Chen, Buxin ;

Newnam, Gary P. ;

Chernoff, Yury O. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (08) :2791-2796

[9] Amyloidogenic domains, prions and structural inheritance: rudiments of early life or recent acquisition? [J].

Chernoff, Y .

CURRENT OPINION IN CHEMICAL BIOLOGY, 2004, 8 (06) :665-671

[10]

Chernoff YO, 1999, MOL CELL BIOL, V19, P8103

← 1 2 3 4 5 →