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Plant Physiol, December 2001, Vol. 127, pp. 1595-1606

Characterization of a Family of Arabidopsis Genes Related to Xyloglucan Fucosyltransferase11

Rodrigo Sarria,2 Tanya A. Wagner, Malcolm A. O'Neill, Ahmed Faik, Curtis G. Wilkerson, Kenneth Keegstra, and Natasha V. Raikhel*

Michigan State University-Department of Energy Plant Research Laboratory (R.S., T.A.W., A.F., C.G.W., K.K., N.V.R.), Departments of Plant Biology (K.K.) and Biochemistry and Molecular Biology (K.K., N.V.R.), Michigan State University, East Lansing, Michigan 48824; and Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, Georgia 30602 (M.A.O.)

To understand primary cell wall assembly in Arabidopsis, we have focused on identifying and characterizing enzymes involved in xyloglucan biosynthesis. Nine genes (AtFUT2-10) were identified that share between 47% and 62% amino acid similarity with the xyloglucan-specific fucosyltransferase AtFUT1. Reverse transcriptase-PCR analysis indicates that all these genes are expressed. Bioinformatic analysis predicts that these family members are fucosyltransferases, and we first hypothesized that some may also be involved in xyloglucan biosynthesis. AtFUT3, AtFUT4, and AtFUT5 were expressed in tobacco (Nicotiana tabacum L. cv BY2) suspension culture cells, and the resulting proteins did not transfer fucose (Fuc) from GDP-Fuc to tamarind xyloglucan. AtFUT3, AtFUT4, and AtFUT5 were overexpressed in Arabidopsis plants. Leaves of plants overexpressing AtFUT4 or AtFUT5 contained more Fuc than wild-type plants. Stems of plants overexpressing AtFUT4 or AtFUT5 contained more xylose, less arabinose, and less galactose than wild-type plants. We suggest that the AtFUT family is likely to include fucosyltransferases important for the synthesis of wall carbohydrates. A targeted analysis of isolated cell wall matrix components from plants altered in expression of these proteins will help determine their specificity and biological function.


1 This work was supported by the National Science Foundation Plant Genome Program (grant no. DBI-9975815), by the Department of Energy Biosciences program (grant no. DE-FG0201ER to K.K. and N.V.R.), and by the Department of Energy (grant nos. DE-FG05-93ER20115 and DE-FG09-93ER20097 to M.A.O.).

2 Present address: BASF Plant Science, L.L.C., 26 Davis Drive, Research Triangle Park, NC 27709.

* Corresponding author; e-mail nraikhel{at}msu.edu; fax 517-353-9168.

© 2001 American Society of Plant Physiologists



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