Coexpression of the soybean vegetative storage protein β subunit (S-VSPβ) either with the bacterial feedback-insensitive dihydrodipicolinate synthase or with S-VSPα stabilizes the S-VSPβ transgene protein and enhances lysine production in transgenic tobacco plants

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עברית

מדריך מקוצר למשתמש מדריך מפורט למשתמש

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הספר "אוצר וולקני"

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פותח על ידי קלירמאש פתרונות בע"מ -

Coexpression of the soybean vegetative storage protein β subunit (S-VSPβ) either with the bacterial feedback-insensitive dihydrodipicolinate synthase or with S-VSPα stabilizes the S-VSPβ transgene protein and enhances lysine production in transgenic tobacco plants

Year: 

2003

Source of publication :

Transgenic Research

Authors :

בדני, חנה

;

גלילי, שמואל

;

גנון (גלברט), דנה

.

Volume :

Co-Authors: 

Guenoune, D., Agronomy/Nat. Resources Department, Agricultural Research Organization, Volcani Center, P.O.B 6, Bet Dagan 50250, Israel
Amir, R., Department of Plant Physiology, Migal Technological Center, Kiryat Shmona 12100, Israel
Badani, H., Agronomy/Nat. Resources Department, Agricultural Research Organization, Volcani Center, P.O.B 6, Bet Dagan 50250, Israel
Wolf, S., Institute of Plant Science, Fac. Agric., Food/Environ. Qual. S., Hebrew University of Jerusalem, Rehovot 76100, Israel
Galili, S., Agronomy/Nat. Resources Department, Agricultural Research Organization, Volcani Center, P.O.B 6, Bet Dagan 50250, Israel

From page: 

123

To page: 

126

(

Total pages: 

4

)

Link :

Abstract: 

Soybean vegetative storage proteins (S-VSPs) are lysine-rich leaf proteins, originally found to accumulate to high levels in depodded soybean plants. In the present study, we overexpressed S-VSPβ, the ruminant stable subunit of the S-VSP genes, in transgenic tobacco plants. The S-VSPβ protein accumulated in all organs studied, but its level declined drastically with leaf age. This instability of S-VSPβ could be overcome either by elevating free lysine levels or by coexpressing S-VSPβ with S-VSPα. High levels of rumen-stable, lysine-rich proteins is expected to improve absorption of lysine by ruminants. Furthermore, the expression of S-VSPs in heterologous plants led to a significant increase in total soluble lysine, suggesting that these proteins may also permit better assimilation of lysine by humans and monogastric animals.