UNSATURATION OF THE MEMBRANE-LIPIDS OF CHLOROPLASTS STABILIZES THE PHOTOSYNTHETIC MACHINERY AGAINST LOW-TEMPERATURE PHOTOINHIBITION IN TRANSGENIC TOBACCO PLANTS
UNSATURATION OF THE MEMBRANE-LIPIDS OF CHLOROPLASTS STABILIZES THE PHOTOSYNTHETIC MACHINERY AGAINST LOW-TEMPERATURE PHOTOINHIBITION IN TRANSGENIC TOBACCO PLANTS
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DOI：
10.1073/pnas.92.14.6219
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发表时间：
1995-07-03
影响因子：
11.1
通讯作者：
MURATA, N
中科院分区：
文献类型：
--
作者：
MOON, BY;HIGASHI, SI;MURATA, N
利用已经用甘油-3-磷酸酰基转移酶的cDNA转化的烟草植物，我们已经证明耐冷性受不饱和膜脂水平的影响。在本研究中，我们检测了用甘油-3-磷酸化的cDNA转化烟草植物的效果，南瓜磷酸酰基转移酶对类囊体膜脂脂肪酸不饱和度的影响以及光合作用对温度的响应。四个主要的脂质类是从类囊体膜，磷脂酰甘油表现出最明显的不饱和度的水平在转化植物的下降。从野生型和转基因植物中分离的类囊体膜在光系统II对高温和低温的敏感性以及光抑制方面没有显着差异。然而，转化植株的叶片比野生型植株对光抑制更敏感。此外，野生型烟草叶片光合作用从光抑制中恢复的速度比转基因烟草叶片快。这些结果表明，磷脂酰甘油在类囊体膜中的脂肪酸的不饱和稳定的光合机械对低温光抑制通过加速恢复的光系统II蛋白复合物。
Using tobacco plants that had been transformed with the cDNA for glycerol-3-phosphate acyltransferase, we have demonstrated that chilling tolerance is affected by the levels of unsaturated membrane lipids, In the present study, we examined the effects of the transformation of tobacco plants with cDNA for glycerol-3-phosphate acyltransferase from squash on the unsaturation of fatty acids in thylakoid membrane lipids and the response of photosynthesis to various temperatures. Of the four major lipid classes is elated from the thylakoid membranes, phosphatidylglycerol showed the most conspicuous decrease in the level of unsaturation in the transformed plants. The isolated thylakoid membranes from wild-type and transgenic plants did not significantly differ from each other in terms of the sensitivity of photosystem II to high and low temperatures and also to photoinhibition. However, leaves of the transformed plants were more sensitive to photoinhibition than those of wild-type plants. Moreover, the recovery of photosynthesis from photoinhibition in leaves of wild-type plants was faster than that in leaves of the transgenic tobacco plants. These results suggest that unsaturation of fatty acids of phosphatidylglycerol in thylakoid membranes stabilizes the photosynthetic machinery against low-temperature photoinhibition by accelerating the recovery of the photosystem II protein complex.