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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 :
12
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
Facilitators :
From page:
123
To page:
126
(
Total pages:
4
)
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.
Note:
Related Files :
Animals
Glycine max
Hydro-Lyases
Improved nutritional quality
Overexpression
Transgenes
עוד תגיות
תוכן קשור
More details
DOI :
10.1023/A:1022130100493
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
23426
Last updated date:
02/03/2022 17:27
Creation date:
16/04/2018 23:59
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Scientific Publication
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
12
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
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
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.
Scientific Publication
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