First published online December 5, 2002; 10.1104/pp.009654
Plant Physiol, December 2002, Vol. 130, pp. 2188-2198
Biosynthesis of UDP-Xylose. Cloning and Characterization of a
Novel Arabidopsis Gene Family, UXS, Encoding Soluble and
Putative Membrane-Bound UDP-Glucuronic Acid Decarboxylase
Isoforms
April D.
Harper and
Maor
Bar-Peled*
Complex Carbohydrate Research Center and Department of Plant
Biology, University of Georgia, 220 Riverbend Road, Athens, Georgia
30602-4712
UDP-xylose (Xyl) is an important sugar donor for
the synthesis of glycoproteins, polysaccharides, various metabolites,
and oligosaccharides in animals, plants, fungi, and bacteria. UDP-Xyl also feedback inhibits upstream enzymes (UDP-glucose [Glc]
dehydrogenase, UDP-Glc pyrophosphorylase, and UDP-GlcA decarboxylase)
and is involved in its own synthesis and the synthesis of
UDP-arabinose. In plants, biosynthesis of UDP-Xyl is catalyzed by
different membrane-bound and soluble UDP-GlcA decarboxylase
(UDP-GlcA-DC) isozymes, all of which convert UDP-GlcA to UDP-Xyl.
Because synthesis of UDP-Xyl occurs both in the cytosol and in
membranes, it is not known which source of UDP-Xyl the different
Golgi-localized xylosyltransferases are utilizing. Here, we describe
the identification of several distinct Arabidopsis genes (named
AtUXS for UDP-Xyl synthase) that encode functional
UDP-GlcA-DC isoforms. The Arabidopsis genome contains five
UXS genes and their protein products can be subdivided into three isozyme classes (A-C), one soluble and two distinct putative membrane bound. AtUxs from each class, when expressed in
Escherichia coli, generate active UDP-GlcA-DC that
converts UDP-GlcA to UDP-Xyl. Members of this gene family have a large conserved C-terminal catalytic domain (approximately 300 amino acids
long) and an N-terminal variable domain differing in sequence and size
(30-120 amino acids long). Isoforms of class A and B appear to encode
putative type II membrane proteins with their catalytic domains facing
the lumen (like Golgi-glycosyltransferases) and their N-terminal
variable domain facing the cytosol. Uxs class C is likely a cytosolic
isoform. The characteristics of the plant Uxs support the hypothesis
that unique UDP-GlcA-DCs with distinct subcellular localizations are
required for specific xylosylation events.
*
Corresponding author; e-mail peled{at}ccrc.uga.edu;
fax 706- 542-4412.
© 2002 American Society of Plant Biologists
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