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Cloning and expression analysis of a UDP-galactose/glucose pyrophosphorylase from melon fruit provides evidence for the major metabolic pathway of galactose metabolism in raffinose oligosaccharide metabolizing plants
Year:
2006
Source of publication :
Plant physiology (source)
Authors :
Dai, Nir
;
.
Katzir, Nurit
;
.
Petreikov, Marina
;
.
Pharr, David M.
;
.
Portnoy, Vitaly H.
;
.
Schaffer, Arthur
;
.
Volume :
142
Co-Authors:
Dai, N., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Petreikov, M., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Portnoy, V., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Katzir, N., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Pharr, D.M., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Schaffer, A.A., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Facilitators :
From page:
294
To page:
304
(
Total pages:
11
)
Abstract:
The Cucurbitaceae translocate a significant portion of their photosynthate as raffinose and stachyose, which are galactosyl derivatives of sucrose. These are initially hydrolyzed by α-galactosidase to yield free galactose (Gal) and, accordingly, Gal metabolism is an important pathway in Cucurbitaceae sink tissue. We report here on a novel plant-specific enzyme responsible for the nucleotide activation of phosphorylated Gal and the subsequent entry of Gal into sink metabolism. The enzyme was antibody purified, sequenced, and the gene cloned and functionally expressed in Escherichia coli. The heterologous protein showed the characteristics of a dual substrate UDP-hexose pyrophosphorylase (PPase) with activity toward both Gal-1-P and glucose (Glc)-1-P in the uridinylation direction and their respective UDP-sugars in the reverse direction. The two other enzymes involved in Glc-P and Gal-P uridinylation are UDP-Glc PPase and uridyltransferase, and these were also cloned, heterologously expressed, and characterized. The gene expression and enzyme activities of all three enzymes in melon (Cucumis melo) fruit were measured. The UDP-Glc PPase was expressed in melon fruit to a similar extent as the novel enzyme, but the expressed protein was specific for Glc-1-P in the UDP-Glc synthesis direction and did not catalyze the nucleotide activation of Gal-1-P. The uridyltransferase gene was only weakly expressed in melon fruit, and activity was not observed in crude extracts. The results indicate that this novel enzyme carries out both the synthesis of UDP-Gal from Gal-1-P as well as the subsequent synthesis of Glc-1-P from the epimerase product, UDP-Glc, and thus plays a key role in melon fruit sink metabolism. © 2006 American Society of Plant Biologists.
Note:
Related Files :
cloning
Cucumis melo
Cucumis sativus
Cucurbitaceae
Genetics
molecular genetics
photosynthesis
Plants
Show More
Related Content
More details
DOI :
10.1104/pp.106.083634
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30768
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:57
Scientific Publication
Cloning and expression analysis of a UDP-galactose/glucose pyrophosphorylase from melon fruit provides evidence for the major metabolic pathway of galactose metabolism in raffinose oligosaccharide metabolizing plants
142
Dai, N., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Petreikov, M., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Portnoy, V., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Katzir, N., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Pharr, D.M., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Schaffer, A.A., Department of Vegetable Research, Agricultural Research Organization, Volcani Center, Bet Dagan, 50250, Israel
Cloning and expression analysis of a UDP-galactose/glucose pyrophosphorylase from melon fruit provides evidence for the major metabolic pathway of galactose metabolism in raffinose oligosaccharide metabolizing plants
The Cucurbitaceae translocate a significant portion of their photosynthate as raffinose and stachyose, which are galactosyl derivatives of sucrose. These are initially hydrolyzed by α-galactosidase to yield free galactose (Gal) and, accordingly, Gal metabolism is an important pathway in Cucurbitaceae sink tissue. We report here on a novel plant-specific enzyme responsible for the nucleotide activation of phosphorylated Gal and the subsequent entry of Gal into sink metabolism. The enzyme was antibody purified, sequenced, and the gene cloned and functionally expressed in Escherichia coli. The heterologous protein showed the characteristics of a dual substrate UDP-hexose pyrophosphorylase (PPase) with activity toward both Gal-1-P and glucose (Glc)-1-P in the uridinylation direction and their respective UDP-sugars in the reverse direction. The two other enzymes involved in Glc-P and Gal-P uridinylation are UDP-Glc PPase and uridyltransferase, and these were also cloned, heterologously expressed, and characterized. The gene expression and enzyme activities of all three enzymes in melon (Cucumis melo) fruit were measured. The UDP-Glc PPase was expressed in melon fruit to a similar extent as the novel enzyme, but the expressed protein was specific for Glc-1-P in the UDP-Glc synthesis direction and did not catalyze the nucleotide activation of Gal-1-P. The uridyltransferase gene was only weakly expressed in melon fruit, and activity was not observed in crude extracts. The results indicate that this novel enzyme carries out both the synthesis of UDP-Gal from Gal-1-P as well as the subsequent synthesis of Glc-1-P from the epimerase product, UDP-Glc, and thus plays a key role in melon fruit sink metabolism. © 2006 American Society of Plant Biologists.
Scientific Publication
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