Evidence for a UDP-glucose transporter in Golgi apparatus-derived vesicles from pea and its possible role in polysaccharide biosynthesis

被引:67
作者
Munoz, P [1 ]
Norambuena, L [1 ]
Orellana, A [1 ]
机构
[1] UNIV CHILE,FAC SCI,DEPT BIOL,SANTIAGO,CHILE
关键词
D O I
10.1104/pp.112.4.1585
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The Golgi apparatus in plant cells is involved in hemicellulose and pectin biosynthesis. While it is known that glucan synthase I is responsible for the formation of beta-1-4-linked glucose (Glc) polymers and uses UDP-Glc as a substrate, very little is known about the topography of reactions leading to the biosynthesis of polysaccharides in this organelle. We isolated from pea (Pisum sativum) stems a fraction highly enriched in Golgi apparatus-derived vesicles that are sealed and have the same topographical orientation that the membranes have in vivo. Using these vesicles and UDP-Glc, we reconstituted polysaccharide biosynthesis in vitro and found evidence for a luminal location of the active site of glucan synthase I. In addition, we identified a UDP-Glc transport activity, which is likely to be involved in supplying substrate for glucan synthase I. We found that UDP-Glc transport is protein mediated. Moreover, our results suggest that UDP-Glc transport is coupled to the exit of a luminal uridine-containing nucleotide via an antiporter mechanism. We suggest that UDP-Glc is transported into the lumen of Golgi and that Glc is transferred to a polysaccharide chain, whereas the nucleotide moiety leaves the vesicle by an antiporter mechanism.
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页码:1585 / 1594
页数:10
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