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First published online April 24, 2003; 10.1104/pp.102.016642 Plant Physiology 132:768-778 (2003) © 2003 American Society of Plant Biologists Analysis of Xyloglucan Fucosylation in Arabidopsis1Michigan State University-Department of Energy Plant Research Laboratory, East Lansing, Michigan (R.M.P., T.A.W., R.S., N.V.R., K.K.); and Complex Carbohydrate Research Center, 220 Riverbend Road, University of Georgia, Athens, Georgia (Z.J., M.A.O., W.S.Y.)
Xyloglucan (XyG) is a load-bearing primary wall component in dicotyledonous and non-graminaceous monocotyledonous plants. XyG fucosyltransferase (FUTase), encoded by the Arabidopsis gene AtFUT1, directs addition of fucose (Fuc) residues to terminal galactose residues on XyG side chains. Reverse transcription-polymerase chain reaction and analysis of promoter-
Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.102.016642. 1 This work was supported by the Department of Energy Biosciences Program and the Plant Genome Program at the National Science Foundation, by the U.S. Department of Energy (grant no. DE–FG05–93ER20220 to Z.J., M.A.O., and W.S.Y.), and by the U.S. Department of Energy-funded Center for Plant and Microbial Complex Carbohydrates (grant no. DE–FG05–93ER20097 to Z.J., M.A.O., and W.S.Y.). 2 Present address: Genetics/Biotechnology Building, Room 3340, 445 Henry Mall, University of Wisconsin, Madison, WI 53706. 3 Present address: BASF Plant Science, 26 Davis Drive, Research Triangle Park, NC 27709. 4 Present address: Center for Plant Cell Biology and Department of Botany and Plant Sciences, Batchelor Hall 2109, University of California, Riverside, CA 92521. * Corresponding author; e-mail keegstra{at}msu.edu; fax 517–353–9168. Received October 25, 2002; returned for revision November 17, 2002; accepted January 15, 2003. This article has been cited by other articles:
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-glucuronidase transgenic plants indicated highest expression of AtFUT1 in the upper portion of elongating inflorescence stems of Arabidopsis. XyG FUTase activity was highest in Golgi vesicles prepared from growing Arabidopsis tissues and low in those isolated from mature tissues. There was no discernible correlation between the Fuc contents of XyG oligosaccharides derived from different Arabidopsis organs and the level of AtFUT1 expression in the organs. Thus, organ-specific variations in AtFUT1 expression and enzyme activity probably reflect differential rates of cell wall biosynthesis, rather than differences in levels of XyG fucosylation. The effects of manipulating AtFUT1 expression were examined using an Arabidopsis mutant (atfut1) containing a T-DNA insertion in the AtFUT1 locus and transgenic plants with strong constitutive expression of AtFUT1. No Fuc was detected in XyG derived from leaves or roots of atfut1. Plants overexpressing AtFUT1 had higher XyG FUTase activity than wild-type plants, but the XyG oligosaccharides derived from the transgenic and wild-type plants contained comparable amounts of Fuc, indicating that suitable acceptor substrates are limiting. Galactosyl residues had slightly higher levels of O-acetylation in XyG from plants that overexpressed AtFUT1 than in XyG from wild-type plants. O-Acetylation of galactose residues was considerably reduced in Fuc-deficient mutants (atfut1, mur1, and mur2) that synthesize XyG containing little or no Fuc. These results suggest that fucosylated XyG is a suitable substrate for at least one O-acetyltransferase in Arabidopsis. 
