Transformation of Arabidopsis thaliana with the codA gene for choline oxidase; accumulation of glycinebetaine and enhanced tolerance to salt and cold stress

被引:332
作者
Hayashi, H
Alia
Mustardy, L
Deshnium, P
Ida, M
Murata, N
机构
[1] NATL INST BASIC BIOL, DEPT REGULAT BIOL, OKAZAKI, AICHI 444, JAPAN
[2] EHIME UNIV, DEPT CHEM, MATSUYAMA, EHIME 790, JAPAN
[3] HUNGARIAN ACAD SCI, BIOL RES CTR, INST PLANT BIOL, H-6701 SZEGED, HUNGARY
[4] NATL INST PHYSIOL SCI, DEPT MOL BIOMECH, OKAZAKI, AICHI 444, JAPAN
关键词
D O I
10.1046/j.1365-313X.1997.12010133.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Glycinebetaine is one of the compatible solutes that accumulate in the chloroplasts of certain halotolerant plants when these plants are exposed to salt or cold stress. The codA gene for choline oxidase, the enzyme that converts choline into glycinebetaine, has previously been cloned from a soil bacterium, Arthrobacter globiformis. Transformation of Arabidopsis thaliana with the cloned codA gene under the control of the 35S promoter of cauliflower mosaic virus enabled the plant to accumulate glycinebetaine and enhanced its tolerance to salt and cold stress. At 300 mM NaCl, considerable proportions of seeds of transformed plants germinated well, whereas seeds of wild-type plants failed to germinate. At 100 mM NaCl, transformed plants grew well whereas wild-type plants did not do so. The transformed plants tolerated 200 mM NaCl, which was lethal to wild-type plants. After plants had been incubated with 400 mM NaCl for two days, the photosystem II activity of wild-type plants had almost completely disappeared, whereas that of transformed plants remained at more than 50% of the original level. When exposed to a low temperature in the light, leaves of wild-type plants exhibited symptoms of chlorosis, whereas those of transformed plants did not. These observations demonstrate that the genetic modification of Arabidopsis thaliana that allowed it to accumulate glycinebetaine enhanced its ability to tolerate salt and cold stress.
引用
收藏
页码:133 / 142
页数:10
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