Carbon-Partitioning in Arabidopsis Is Regulated by the Fructose 6-Phosphate, 2-Kinase/Fructose 2,6-Bisphosphatase Enzyme

To further elucidate the mechanisms underlying carbon-partitioning in plants, we established an experimental system by generating transgenic Arabidopsis lines that overexpress both the fructose 6-phosphate, 2-kinase (F6P,2-K) and the fructose 2,6-bisphosphatase (F26BPase) domains. We also produced k...

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Published in:Journal of plant biology = Singmul Hakhoe chi 2006-02, Vol.49 (1)
Main Authors: Lee, Y.H. (Kyung Hee University, Suwon, Republic of Korea), Lee, D.S. (Kyung Hee University, Suwon, Republic of Korea), Lim, J.M. (Kyung Hee University, Suwon, Republic of Korea), Yoon, J.M. (Kyung Hee University, Suwon, Republic of Korea), Bhoo, S.H. (Kyung Hee University, Suwon, Republic of Korea), Jeon, J.S. (Kyung Hee University, Suwon, Republic of Korea), Hahn, T.R. (Kyung Hee University, Suwon, Republic of Korea), E-mail: trhahn@khu.ac.kr
Format: Article
Language:English
Subjects:
2-kinase/fructose 2,6-bisphosphatase
ARABIDOPSIS
carbohydrate metabolites
carbon-partitioning
fructose 2,6-bisphosphate
fructose 6-phosphate
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Summary:To further elucidate the mechanisms underlying carbon-partitioning in plants, we established an experimental system by generating transgenic Arabidopsis lines that overexpress both the fructose 6-phosphate, 2-kinase (F6P,2-K) and the fructose 2,6-bisphosphatase (F26BPase) domains. We also produced knockout transgenic plants for these domains via RNAi and T-DNA tagging. In F6P,2-K overexpressing transgenics, F6P,2-K activity increased slightly and Fru-2,6-Pâ‚‚ levels were elevated by 80%, compared with the wild type (WT). F26BPase activity was similar between the WT and transgenic plants.
ISSN:1226-9239
1867-0725
DOI:10.1007/BF03030790