The yeast prion protein Ure2: Structure, function and folding

被引：28

作者：

Lian, HY

Jiang, Y

Zhang, H

Jones, GW

Perrett, S

机构：

[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China

[2] Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China

[3] Natl Univ Ireland, Dept Biol, Maynooth, Kildare, Ireland

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2006年 / 1764卷 / 03期

基金：

中国国家自然科学基金;

关键词：

prion; amyloid; glutathione transferase; peroxidase; Protein Folding; chaperone;

D O I：

10.1016/j.bbapap.2005.11.016

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The Saccharomyces cerevisiae protein Ure2 functions as a regulator of nitrogen metabolism and as a glutathione-dependent peroxidase. Ure2 also has the characteristics of a prion, in that it can undergo a heritable conformational change to an aggregated state,, the prion form of Ure2 loses the regulatory function, but the enzymatic function appears to be maintained. A number of factors are found to affect the prion properties of Ure2, including mutation and expression levels of molecular chaperones, and the effect of these factors oil structure and stability are being investigated. The relationship between structure, function and folding for the yeast prion Ure2 are discussed. (c) 2005 Elsevier B.V. All rights reserved.

引用

收藏

页码：535 / 545

页数：11

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