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

FEBS Letters

Downs, Craig A¹  Heckathorn, Scott A¹ 

[1] Department of Biology, University of Charleston, 58 Coming Street, Charleston, SC 29424, USA

关键词: Small heat-shock protein;    Mitochondrion;    Oxidative phosphorylation;    Heat stress;    lmw Hsp;    low-molecular-weight heat-shock protein;   

DOI  :  10.1016/S0014-5793(98)00669-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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:O₂ 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 lmw Hsp is an important adaptation to heat stress in plants.

【 授权许可】

Unknown