Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response

被引:2193
作者
Wang, WX
Vinocur, B
Shoseyov, O
Altman, A
机构
[1] Hebrew Univ Jerusalem, Robert H Smith Inst Plant Sci & Genet Agr, Fac Agr Food & Environm Qual Sci, IL-76100 Rehovot, Israel
[2] Hebrew Univ Jerusalem, Otto Warburg Ctr Agr Biotechnol, Fac Agr Food & Environm Qual Sci, IL-76100 Rehovot, Israel
关键词
D O I
10.1016/j.tplants.2004.03.006
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Abiotic stresses usually cause protein dysfunction. Maintaining proteins in their functional conformations and preventing the aggregation of non-native proteins are particularly important for cell survival under stress. Heat-shock proteins (Hsps)/chaperones are responsible for protein folding, assembly, translocation and degradation in many normal cellular processes, stabilize proteins and membranes, and can assist in protein refolding under stress conditions. They can play a crucial role in protecting plants against stress by reestablishing normal protein conformation and thus cellular homeostasis. Here, we summarize the significance of Hsps and chaperones in abiotic stress responses in plants, and discuss the co-operation among their different classes and their interactions with other stress-induced components.
引用
收藏
页码:244 / 252
页数:9
相关论文
共 102 条
[21]  
Easton DP, 2000, CELL STRESS CHAPERON, V5, P276, DOI 10.1379/1466-1268(2000)005<0276:THAGSP>2.0.CO
[22]  
2
[23]   Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation [J].
Ehrnsperger, M ;
Graber, S ;
Gaestel, M ;
Buchner, J .
EMBO JOURNAL, 1997, 16 (02) :221-229
[24]   Folding of newly translated proteins in vivo: The role of molecular chaperones [J].
Frydman, J .
ANNUAL REVIEW OF BIOCHEMISTRY, 2001, 70 :603-647
[25]   Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins [J].
Glover, JR ;
Lindquist, S .
CELL, 1998, 94 (01) :73-82
[26]   Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network [J].
Goloubinoff, P ;
Mogk, A ;
Ben Zvi, AP ;
Tomoyasu, T ;
Bukau, B .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (24) :13732-13737
[27]   CONSERVATION OF THE REGULATORY SUBUNIT FOR THE CLP ATP-DEPENDENT PROTEASE IN PROKARYOTES AND EUKARYOTES [J].
GOTTESMAN, S ;
SQUIRES, C ;
PICHERSKY, E ;
CARRINGTON, M ;
HOBBS, M ;
MATTICK, JS ;
DALRYMPLE, B ;
KURAMITSU, H ;
SHIROZA, T ;
FOSTER, T ;
CLARK, WP ;
ROSS, B ;
SQUIRES, CL ;
MAURIZI, MR .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (09) :3513-3517
[28]   Group II chaperonins: New TRiC(k)s and turns of a protein folding machine [J].
Gutsche, I ;
Essen, LO ;
Baumeister, F .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 293 (02) :295-312
[29]   The organization and evolution of the spinach stress 70 molecular chaperone gene family [J].
Guy, CL ;
Li, QB .
PLANT CELL, 1998, 10 (04) :539-556
[30]   Mitochondrial adaptations to NaCl. Complex I is protected by anti-oxidants and small heat shock proteins, whereas complex II is protected by proline and betaine [J].
Hamilton, EW ;
Heckathorn, SA .
PLANT PHYSIOLOGY, 2001, 126 (03) :1266-1274