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A soybean vegetative storage protein accumulates to high levels in various organs of transgenic tobacco plants
Year:
1999
Source of publication :
Plant Science
Authors :
Ben-Dor, Bruria
;
.
Galili, Shmuel
;
.
Guenoune (Gelbart), Dana
;
.
Volume :
145
Co-Authors:
Guenoune, D., Department of Field and Garden Crops, Agric. Res. Org. (Volcani Ctr.), P., Bet-Dagan, Israel
Amir, R., Department of Plant Physiology, Migal Technological Center, Kiryat Shmona, Israel
Ben-Dor, B., Department of Field and Garden Crops, Agric. Res. Org. (Volcani Ctr.), P., Bet-Dagan, Israel
Wolf, S., Department of Field Crops, Vegetables Genet. Otto Warburg C., Rehovot, Israel
Galili, S., Department of Field and Garden Crops, Agric. Res. Org. (Volcani Ctr.), P., Bet-Dagan, Israel
Facilitators :
From page:
93
To page:
98
(
Total pages:
6
)
Abstract:
Soybean vegetative storage proteins (S-VSPs) are a group of high-lysine proteins. These proteins can accumulate up to 15% of the soluble leaf proteins in young shoots, as well as in shoots of depodded mature plants. Closely related proteins are found in forage crops, such as alfalfa. We have expressed the S-VSPα gene, fused to the strong constitutive cauliflower mosaic virus 35S promoter, in transgenic tobacco as a model plant to study the potential of producing high levels of S-VSPs for the nutritional improvement of forage crops. S-VSPα was detected in the soluble (albumin) fraction of the transgenic plants. The transgenic protein migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis similarly to the natural S-VSPα of soybean, suggesting that it was correctly processed in tobacco and accumulated in the vacuoles. The S-VSPα ranged between 2 and 6% of the soluble proteins in leaves of the transgenic plants and was present in various organs and in mature leaves. Our results suggest that S-VSPs can serve as an excellent protein source for improving the nutritional quality of crop plants, particularly cereal forage and grains, which contain limiting levels of lysine.
Note:
Related Files :
Cauliflower mosaic virus
gene expression
Improved quality
Overexpression
soybean
transgenic plants
Show More
Related Content
More details
DOI :
10.1016/S0168-9452(99)00079-5
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
31071
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:59
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Scientific Publication
A soybean vegetative storage protein accumulates to high levels in various organs of transgenic tobacco plants
145
Guenoune, D., Department of Field and Garden Crops, Agric. Res. Org. (Volcani Ctr.), P., Bet-Dagan, Israel
Amir, R., Department of Plant Physiology, Migal Technological Center, Kiryat Shmona, Israel
Ben-Dor, B., Department of Field and Garden Crops, Agric. Res. Org. (Volcani Ctr.), P., Bet-Dagan, Israel
Wolf, S., Department of Field Crops, Vegetables Genet. Otto Warburg C., Rehovot, Israel
Galili, S., Department of Field and Garden Crops, Agric. Res. Org. (Volcani Ctr.), P., Bet-Dagan, Israel
A soybean vegetative storage protein accumulates to high levels in various organs of transgenic tobacco plants
Soybean vegetative storage proteins (S-VSPs) are a group of high-lysine proteins. These proteins can accumulate up to 15% of the soluble leaf proteins in young shoots, as well as in shoots of depodded mature plants. Closely related proteins are found in forage crops, such as alfalfa. We have expressed the S-VSPα gene, fused to the strong constitutive cauliflower mosaic virus 35S promoter, in transgenic tobacco as a model plant to study the potential of producing high levels of S-VSPs for the nutritional improvement of forage crops. S-VSPα was detected in the soluble (albumin) fraction of the transgenic plants. The transgenic protein migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis similarly to the natural S-VSPα of soybean, suggesting that it was correctly processed in tobacco and accumulated in the vacuoles. The S-VSPα ranged between 2 and 6% of the soluble proteins in leaves of the transgenic plants and was present in various organs and in mature leaves. Our results suggest that S-VSPs can serve as an excellent protein source for improving the nutritional quality of crop plants, particularly cereal forage and grains, which contain limiting levels of lysine.
Scientific Publication
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