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
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
收藏
页码:630 / 634
页数:5
相关论文
共 20 条
[1]   Inventory, evolution and expression profiling diversity of the LEA (late embryogenesis abundant) protein gene family in Arabidopsis thaliana [J].
Bies-Etheve, Natacha ;
Gaubier-Comella, Pascale ;
Debures, Anne ;
Lasserre, Eric ;
Jobet, Edouard ;
Raynal, Monique ;
Cooke, Richard ;
Delseny, Michel .
PLANT MOLECULAR BIOLOGY, 2008, 67 (1-2) :107-124
[2]   MtPM25 is an atypical hydrophobic late embryogenesis-abundant protein that dissociates cold and desiccation-aggregated proteins [J].
Boucher, Virginie ;
Buitink, Julia ;
Lin, Xiaodong ;
Boudet, Julie ;
Hoekstra, Folkert A. ;
Hundertmark, Michaela ;
Renard, Denis ;
Leprince, Olivier .
PLANT CELL AND ENVIRONMENT, 2010, 33 (03) :418-430
[3]   Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae [J].
Browne, JA ;
Dolan, KM ;
Tyson, T ;
Goyal, K ;
Tunnacliffe, A ;
Burnell, AM .
EUKARYOTIC CELL, 2004, 3 (04) :966-975
[4]   Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function [J].
Chakrabortee, Sohini ;
Boschetti, Chiara ;
Walton, Laura J. ;
Sarkar, Sovan ;
Rubinsztein, David C. ;
Tunnacliffe, Alan .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (46) :18073-18078
[5]   Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance [J].
Chakrabortee, Sohini ;
Meersman, Filip ;
Schierle, Gabriele S. Kaminski ;
Bertoncini, Carlos W. ;
McGee, Brian ;
Kaminski, Clemens F. ;
Tunnacliffe, Alan .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2010, 107 (37) :16084-16089
[6]   LEA proteins prevent protein aggregation due to water stress [J].
Goyal, K ;
Walton, LJ ;
Tunnacliffe, A .
BIOCHEMICAL JOURNAL, 2005, 388 :151-157
[7]   Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein [J].
Goyal, K ;
Tisi, L ;
Basran, A ;
Browne, J ;
Burnell, A ;
Zurdo, J ;
Tunnacliffe, A .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (15) :12977-12984
[8]   LEA (Late Embryogenesis Abundant) proteins and their encoding genes in Arabidopsis thaliana [J].
Hundertmark, Michaela ;
Hincha, Dirk K. .
BMC GENOMICS, 2008, 9 (1)
[9]   Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins [J].
Kovacs, Denes ;
Kalmar, Eva ;
Torok, Zsolt ;
Tompa, Peter .
PLANT PHYSIOLOGY, 2008, 147 (01) :381-390
[10]  
LeVine H, 1999, METHOD ENZYMOL, V309, P274