Glycobiology, 2000, Vol. 10, No. 6 611-621
© 2000 Oxford University Press
Three bovine 
2-fucosyltransferase genes encode enzymes that preferentially transfer fucose on Galß1–3GalNAc acceptor substrates
2Unité de Génétique Moléculaire Animale-UMR 1061 (INRA/Université de Limoges) Institut Sciences de la Vie et de la Santé, Faculté des Sciences, 87060 Limoges, France, 3Laboratoire de Génétique Biochimique et Cytogénétique, INRA-CRJ, 78350 Jouy-en-Josas, France, and 4Glycobiologie INSERM U 504 / Université Paris Sud XI, 94807 Villejuif, France
To investigate the synthesis of 
2-fucosylated epitopes in the bovine species, we have characterized cDNAs from various tissues. We found three distinct 2-fucosyltransferase genes, named bovine fut1, fut2, and sec1 which are homologous to human FUT1, FUT2, and Sec1 genes, respectively. Their open reading frames (ORF) encode polypeptides of 360 (bovine H), 344 (bovine Se), and 368 (bovine Sec1) amino acids, respectively. These enzymes transfer fucose in 1,2 linkage to ganglioside GM1 and galacto-N-biose, but not to the phenyl-ß-D-galactoside, type 1 or type 2 acceptors, suggesting that their substrate specificity is different and more restricted than the other cloned mammalian 2-fucosyltransferases. Southern blot analyses detected four related 2-fucosyltransferase sequences in the bovine genome while only three have been described in other species. The supernumerary entity seems to be related to the 2-fucosyltransferase activity which can also use type 1 and phenyl-ß-D-galactoside substrate acceptors. It was exclusively found in bovine intestinal tract. Our results show that, at least in one mammalian species, four 2-fucosyltransferases are present, three adding a fucose on 1,2 linkage on type 3/4 acceptor (Galß1–3GalNAc) and another able to transfer also fucose on phenyl-ß-D-galactoside and type 1 (Galß1–3GlcNAc) acceptors. The phylogenetic tree of the enzymes homologous to those encoded by the bovine fut1, fut2, and sec1 genes revealed two main families, one containing all the H-like proteins and the second containing all the Se-like and Sec1-like proteins. The Sec1-like family had a higher evolutionary rate than the Se-like family.
1 To whom correspondence should be addressed at: Bâtiment de Biotechnologie, Faculté des Sciences, 123 avenue Albert Thomas, F-87060 Limoges, France
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