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First published online October 20, 2006; 10.1105/tpc.105.036566

The Plant Cell 18:2593-2607 (2006)
© 2006 American Society of Plant Biologists

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Arabidopsis thaliana RGXT1 and RGXT2 Encode Golgi-Localized (1,3)-{alpha}-D-Xylosyltransferases Involved in the Synthesis of Pectic Rhamnogalacturonan-II[W],[OA]

Jack Egelunda, Bent Larsen Petersena, Mohammed Saddik Motawiab, Iben Damagera, Ahmed Faikc,1, Carl Erik Olsend, Tadashi Ishiie, Henrik Clausenf, Peter Ulvskova and Naomi Geshia,2,3

a Biotechnology Group, Danish Institute of Agricultural Sciences and Center for Molecular Plant Physiology, DK-1871 Frederiksberg C, Denmark
b Plant Biochemistry Laboratory, Department of Plant Biology and Center for Molecular Plant Physiology, Royal Veterinary and Agricultural University, DK-1871 Frederiksberg C, Denmark
c Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824
d Department of Natural Sciences and Center for Molecular Plant Physiology, Royal Veterinary and Agricultural University, DK-1871 Frederiksberg C, Denmark
e Forestry and Forest Research Institute, Tsukuba Norin Kenkyu Danchi-nai, Ibaraki 305-8687, Japan
f Department of Medical Biochemistry and Genetics, University of Copenhagen, DK-2200 Copenhagen N, Denmark

3 To whom correspondence should be addressed. E-mail nge{at}kvl.dk; fax 45-35283333.

Two homologous plant-specific Arabidopsis thaliana genes, RGXT1 and RGXT2, belong to a new family of glycosyltransferases (CAZy GT-family-77) and encode cell wall (1,3)-{alpha}-D-xylosyltransferases. The deduced amino acid sequences contain single transmembrane domains near the N terminus, indicative of a type II membrane protein structure. Soluble secreted forms of the corresponding proteins expressed in insect cells showed xylosyltransferase activity, transferring D-xylose from UDP-{alpha}-D-xylose to L-fucose. The disaccharide product was hydrolyzed by {alpha}-xylosidase, whereas no reaction was catalyzed by ß-xylosidase. Furthermore, the regio- and stereochemistry of the methyl xylosyl-fucoside was determined by nuclear magnetic resonance to be an {alpha}-(1,3) linkage, demonstrating the isolated glycosyltransferases to be (1,3)-{alpha}-D-xylosyltransferases. This particular linkage is only known in rhamnogalacturonan-II, a complex polysaccharide essential to vascular plants, and is conserved across higher plant families. Rhamnogalacturonan-II isolated from both RGXT1 and RGXT2 T-DNA insertional mutants functioned as specific acceptor molecules in the xylosyltransferase assay. Expression of RGXT1- and RGXT2-enhanced green fluorescent protein constructs in Arabidopsis revealed that both fusion proteins were targeted to a Brefeldin A–sensitive compartment and also colocalized with the Golgi marker dye BODIPY TR ceramide, consistent with targeting to the Golgi apparatus. Taken together, these results suggest that RGXT1 and RGXT2 encode Golgi-localized (1,3)-{alpha}-D-xylosyltransferases involved in the biosynthesis of pectic rhamnogalacturonan-II.




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