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First published online August 16, 2002; 10.1104/pp.003400

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Plant Physiol, September 2002, Vol. 130, pp. 432-441

Arabinoxylan Biosynthesis in Wheat. Characterization of Arabinosyltransferase Activity in Golgi Membranes1

Andrea Celia Porchia,2 Susanne Oxenbøll Sørensen, and Henrik Vibe Scheller*

Plant Biochemistry Laboratory, Department of Plant Biology, The Royal Veterinary and Agricultural University, 1871 Frederiksberg C, Copenhagen, Denmark

Arabinoxylan arabinosyltransferase (AX-AraT) activity was investigated using microsomes and Golgi vesicles isolated from wheat (Triticum aestivum) seedlings. Incubation of microsomes with UDP-[14C]-beta -L-arabinopyranose resulted in incorporation of radioactivity into two different products, although most of the radioactivity was present in xylose (Xyl), indicating a high degree of UDP-arabinose (Ara) epimerization. In isolated Golgi vesicles, the epimerization was negligible, and incubation with UDP-[14C]Ara resulted in formation of a product that could be solubilized with proteinase K. In contrast, when Golgi vesicles were incubated with UDP-[14C]Ara in the presence of unlabeled UDP-Xyl, the product obtained could be solubilized with xylanase, whereas proteinase K had no effect. Thus, the AX-AraT is dependent on the synthesis of unsubstituted xylan acting as acceptor. Further analysis of the radiolabeled product formed in the presence of unlabeled UDP-Xyl revealed that it had an apparent molecular mass of approximately 500 kD. Furthermore, the total incorporation of [14C]Ara was dependent on the time of incubation and the amount of Golgi protein used. AX-AraT activity had a pH optimum at 6, and required the presence of divalent cations, Mn2+ being the most efficient. In the absence of UDP-Xyl, a single arabinosylated protein with an apparent molecular mass of 40 kD was radiolabeled. The [14C]Ara labeling became reversible by adding unlabeled UDP-Xyl to the reaction medium. The possible role of this protein in arabinoxylan biosynthesis is discussed.

1 This work was supported by the Danish National Research Foundation and by the Danish Ministry of Food.

2 Present address: Pharmexa, Kogle Allé 6, DK-2970 Hørsholm, Denmark.

* Corresponding author; e-mail hvs{at}kvl.dk; fax 45-35283333.

© 2002 American Society of Plant Physiologists


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