Glycobiology, 2002, Vol. 12, No. 5 299-306
© 2002 Oxford University Press
The presence of Lewis a epitopes in Arabidopsis thaliana glycoconjugates depends on an active 
4-fucosyltransferase gene
2 Equipe de Glycobiologie et Biotechnologie (EA 3176), Institut des Sciences de la Vie et de la Santé, Université de Limoges, Faculté des Sciences, 123, Avenue Albert Thomas, 87060 Limoges, France; 3 Laboratoire de Physiologie et de Biochimie Végétales URA CNRS 571, Université de Poitiers, 25 rue du Faubourg St Cyprien, 86000, Poitiers, France; and 4 Laboratoire des transports intracellulaires, CNRS UMR 6037, IFRMP 23 Université de Rouen, UFR des Sciences, 76821 Mont St Aignan, Cedex, France
The presence of an 
4-fucosyltransferase in plants was first deduced from the characterization of Lewis-a glycoepitopes in some N-glycans. The first plant gene encoding an 4-fucosyltransferase was recently cloned in Beta vulgaris. In the present paper we provide evidence for the presence of an 4-fucosyltransferase in A. thaliana by measurement of this glycosyltransferase activity from a purified microsomal preparation and by immunolocalization of Lea epitopes on glycans N-linked to glycoproteins located to the Golgi apparatus and on the cell surface. The corresponding gene AtFT4 (AY026941) was characterized. A unique copy of this gene was found in A. thaliana genome, and a single AtFT4 transcript was revealed in leaves, in roots, and at a lower extent in flowers. The coding sequence of AtFT4 gene is interrupted by two introns spanning 465 bp and 84 bp, respectively. The putative 393-amino-acid protein (44 kDa, pI: 6.59) contains an N-terminal hydrophobic region and one potential N-glycosylation site, but AtFT4 has poor homology (less than 30%) to the other 3/4-fucosyltransferases except for motif II. When expressed in COS 7 cells the protein is able to transfer Fuc from GDP-Fuc to a type 1 acceptor substrate, but this transferase activity is detected only in the culture medium of transfected cells
1 To whom correspondence should be addressed
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