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Originally published In Press as doi:10.1074/jbc.M000677200 on March 9, 2000
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J Biol Chem, Vol. 275, Issue 20, 15082-15089, May 19, 2000

Biochemical Characterization and Molecular Cloning of an alpha -1,2-Fucosyltransferase That Catalyzes the Last Step of Cell Wall Xyloglucan Biosynthesis in Pea*

Ahmed FaikDagger , Maor Bar-PeledDagger §, Amy E. DeRocherDagger , Weiqing ZengDagger ||, Robyn M. PerrinDagger **, Curtis WilkersonDagger , Natasha V. RaikhelDagger Dagger Dagger , and Kenneth KeegstraDagger **Dagger Dagger §§

From the Dagger  Department of Energy Plant Research Laboratory, the || Cell and Molecular Biology Program, the ** Department of Botany and Plant Pathology, and the Dagger Dagger  Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824

Pea microsomes contain an alpha -fucosyltransferase that incorporates fucose from GDP-fucose into xyloglucan, adding it preferentially to the 2-O-position of the galactosyl residue closest to the reducing end of the repeating subunit. This enzyme was solubilized with detergent and purified by affinity chromatography on GDP-hexanolamine-agarose followed by gel filtration. By utilizing peptide sequences obtained from the purified enzyme, a cDNA clone was isolated that encodes a 565-amino acid protein with a predicted molecular mass of 64 kDa and shows 62.3% identity to its Arabidopsis homolog. The purified transferase migrates at ~63 kDa by SDS-polyacrylamide gel electrophoresis but elutes from the gel filtration column as an active protein of higher molecular weight (~250 kDa), indicating that the active form is an oligomer. The enzyme is specific for xyloglucan and is inhibited by xyloglucan oligosaccharides and by the by-product GDP. The enzyme has a neutral pH optimum and does not require divalent ions. Kinetic analysis indicates that GDP-fucose and xyloglucan associate with the enzyme in a random order. N-Ethylmaleimide, a cysteine-specific modifying reagent, had little effect on activity, although several other amino acid-modifying reagents strongly inhibited activity.

* This work was supported by the United States Department of Energy.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF223643.

§ Present address: Washington University School of Medicine, Dept. of Molecular Microbiology, Campus Box 8230, 660 South Euclid Ave., St. Louis, MO 63110-1093.

Present address: Seattle Biomedical Research Institute, 4 Nickerson St., Suite 200, Seattle, WA 98109.

§§ To whom correspondence should be addressed. Tel.: 517-353-7874; Fax: 517-353-9168; E-mail: keegstra@msu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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