First published online January 23, 2003; 10.1105/tpc.008425
The Plant Cell, Vol. 15, 523-531,
February 2003, Copyright © 2003,
American Society of Plant Biologists
The Biosynthesis of L-Arabinose in Plants
Molecular Cloning and Characterization of a Golgi-Localized UDP-D-Xylose 4-Epimerase Encoded by the MUR4 Gene of Arabidopsis
Emilie G. Burget,
Rajeev Verma,
Michael Mølhøj and
Wolf-Dieter Reiter1
Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269
1 To whom correspondence should be addressed. E-mail wdreiter{at}uconnvm.uconn.edu; fax 860-486-4331
The mur4 mutant of Arabidopsis shows a 50% reduction in the monosaccharide L-Ara in leaf-derived cell wall material because of a partial defect in the 4-epimerization of UDP-D-Xyl to UDP-L-Ara. To determine the genetic lesion underlying the mur4 phenotype, the MUR4 gene was cloned by a map-based procedure and found to encode a type-II membrane protein with sequence similarity to UDP-D-Glc 4-epimerases. Enzyme assays of MUR4 protein expressed in the methylotropic yeast Pichia pastoris indicate that it catalyzes the 4-epimerization of UDP-D-Xyl to UDP-L-Ara, the nucleotide sugar used by glycosyltransferases in the arabinosylation of cell wall polysaccharides and wall-resident proteoglycans. Expression of MUR4green fluorescent protein constructs in Arabidopsis revealed localization patterns consistent with targeting to the Golgi, suggesting that the MUR4 protein colocalizes with glycosyltransferases in the biosynthesis of arabinosylated cell wall components. The Arabidopsis genome encodes three putative proteins with >76% sequence identity to MUR4, which may explain why mur4 plants are not entirely deficient in the de novo synthesis of UDP-L-Ara.
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