Downs C A, Heckathorn S A
Department of Biology, University of Charleston, SC 29424, USA.
FEBS Lett. 1998 Jul 3;430(3):246-50. doi: 10.1016/s0014-5793(98)00669-3.
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.
利用蛋白质特异性抗体使线粒体小热休克蛋白（低分子量热休克蛋白）在亚线粒体小泡中功能失活，结果表明该蛋白可保护NADH：泛醌氧化还原酶（复合体I），从而保护从复合体I到细胞色素c：O2氧化还原酶（复合体IV）的电子传递。低分子量热休克蛋白的功能完全解释了预热胁迫植物中复合体I电子传递的热适应现象。将纯化的低分子量热休克蛋白添加到缺乏该热休克蛋白的亚线粒体小泡中，在高温下测定的亚线粒体小泡中，复合体I的电子传递速率提高了100%。这些结果表明，线粒体低分子量热休克蛋白的产生是植物对热胁迫的一种重要适应性反应。
