The mitochondrial small heat-shock protein protects NADH:ubiquinone oxidoreductase of the electron transport chain during heat stress in plants

被引：112

作者：

Downs, CA ^{[1
]}

Heckathorn, SA ^{[1
]}

机构：

[1] Univ Charleston, Dept Biol, Charleston, SC 29424 USA

来源：

FEBS LETTERS | 1998年 / 430卷 / 03期

基金：

美国国家科学基金会;

关键词：

small heat-shock protein; mitochondrion; oxidative phosphorylation; heat stress;

D O I：

10.1016/S0014-5793(98)00669-3

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：

Functional inactivation of the mitochondrial small heat-shock protein (lmw Hsp) in submitochondrial vesicles using protein-specific antibodies indicated that this protein protects NADH:ubiquinone oxidoreductase (complex I), and consequently electron transport from complex I to cytochrome c:O(2) oxidoreductase (complex IV). Lmw Hsp function completely accounted for heat acclimation of complex I electron transport in pre-heat-stressed plants. Addition of purified lmw Hsp to submitochondrial vesicles lacking this Hsp increased complex I electron transport rates 100% in submitochondrial vesicles assayed at high temperatures. These results indicate that production of the mitochondrial Imw Hsp is an important adaptation to heat stress in plants. (C) 1998 Federation of European Biochemical Societies.

引用

页码：246 / 250

页数：5

共 35 条

[1] EFFECTS OF THE OVEREXPRESSION OF THE SMALL HEAT-SHOCK PROTEIN, HSP27, ON THE SENSITIVITY OF HUMAN FIBROBLAST CELLS EXPOSED TO OXIDATIVE STRESS [J].