Both plant and animal LEA proteins act as kinetic stabilisers of polyglutamine-dependent protein aggregation

被引：40

作者：

Liu, Yun ^{[1
]}

Chakrabortee, Sohini ^{[2
]}

Li, Ranhui ^{[1
]}

Zheng, Yizhi ^{[1
]}

Tunnacliffe, Alan ^{[2
]}

机构：

[1] Shenzhen Univ, Sch Life Sci, Shenzhen 518060, Guangdong, Peoples R China

[2] Univ Cambridge, Dept Chem Engn & Biotechnol, Cambridge CB2 1QT, England

来源：

FEBS LETTERS | 2011年 / 585卷 / 04期

基金：

中国国家自然科学基金; 欧洲研究理事会;

关键词：

Molecular shield; Protein homeostasis; Proteostasis; Desiccation tolerance; Anhydrobiosis; Cold tolerance; EMBRYOGENESIS-ABUNDANT PROTEIN; DESICCATION TOLERANCE; STRESS;

D O I：

10.1016/j.febslet.2011.01.020

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：

LEA (late embryogenesis abundant) proteins are intrinsically disordered proteins that contribute to stress tolerance in plants and invertebrates. Here we show that, when both plant and animal LEA proteins are co-expressed in mammalian cells with self-aggregating polyglutamine (polyQ) proteins, they reduce aggregation in a time-dependent fashion, showing more protection at early time points. A similar effect was also observed in vitro, where recombinant LEA proteins were able to slow the rate of polyQ aggregation, but not abolish it altogether. Thus, LEA proteins act as kinetic stabilisers of aggregating proteins, a novel function in protein homeostasis consistent with a proposed role as molecular shields. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：630 / 634

页数：5

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