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Plant Physiol, March 2000, Vol. 122, pp. 867-878
GDP-Fucose Uptake into the Golgi Apparatus during Xyloglucan
Biosynthesis Requires the Activity of a Transporter-Like Protein Other
Than the UDP-Glucose Transporter1
Cristian
Wulff,2
Lorena
Norambuena,2 and
Ariel
Orellana*
Department of Biology, Faculty of Sciences, University of Chile,
Casilla 653, Santiago, Chile
The
molecular mechanisms regulating hemicelluloses and pectin biosynthesis
are poorly understood. An important question in this regard is how
glycosyltransferases are oriented in the Golgi cisternae, and how
nucleotide sugars are made available for the synthesis of the polymers.
Here we show that the branching enzyme xyloglucan  ,1-2
fucosyltransferase (XG-FucTase) from growing pea (Pisum
sativum) epicotyls was latent and protected against proteolytic
inactivation on intact, right-side-in pea stem Golgi vesicles.
Moreover, much of the XG-FucTase activity was membrane associated.
These data indicate that XG-FucTase is a membrane-bound luminal enzyme.
GDP-Fuc uptake studies demonstrated that GDP-Fuc was taken up into
Golgi vesicles in a protein-mediated process, and that this uptake was
not competed by UDP-Glc, suggesting that a specific GDP-Fuc transporter
is involved in xyloglucan biosynthesis. Once in the lumen, Fuc was
transferred onto endogenous acceptors, including xyloglucan. GDPase
activity was detected in the lumen of the vesicles, suggesting than the
GDP produced upon transfer of Fuc was hydrolyzed to GMP and inorganic
phosphate. We suggest than the GDP-Fuc transporter and GDPase may be
regulators of xyloglucan fucosylation in the Golgi apparatus from pea epicotyls.
1
This work was supported by Fondecyt grant
no. 1970494, Chile.
2
These authors contributed equally to the paper.
*
Corresponding author; e-mail Aorellan{at}Abello.dic.uchile.cl;
fax 56-2-2712983.
© 2000 American Society of Plant Physiologists
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