title: The α1,6-fucosyltransferase gene (fut8) from the Sf9 lepidopteran insect cell line: insights into fut8 evolution.
abstract: The core alpha1,6-fucosyltransferase (FUT8) catalyzes the transfer of a fucosyl moiety from GDP-fucose to the innermost asparagine-linked N-acetylglucosamine residue of glycoproteins. In mammals, this glycosylation has an important function in many fundamental biological processes and although no essential role has been demonstrated yet in all animals, FUT8 amino acid (aa) sequence and FUT8 activity are very well conserved throughout the animal kingdom. We have cloned the cDNA and the complete gene encoding the FUT8 in the Sf9 (Spodoptera frugiperda) lepidopteran cell line. As in most animal genomes, fut8 is a single-copy gene organized in different exons. The open reading frame contains 12 exons, a characteristic that seems to be shared by all lepidopteran fut8 genes. We chose to study the gene structure as a way to characterize the evolutionary relationships of the fut8 genes in metazoans. Analysis of the intron-exon organization in 56 fut8 orthologs allowed us to propose a model for fut8 evolution in metazoans. The presence of a highly variable number of exons in metazoan fut8 genes suggests a complex evolutionary history with many intron gain and loss events, particularly in arthropods, but not in chordata. Moreover, despite the high conservation of lepidoptera FUT8 sequences also in vertebrates and hymenoptera, the exon-intron organization of hymenoptera fut8 genes is order-specific with no shared exons. This feature suggests that the observed intron losses and gains may be linked to evolutionary innovations, such as the appearance of new orders.
authors.affiliation: CNRS UPS3044 Baculovirus et Thérapie, Saint Christol Lèz Alès, France.
authors.forename: Sylvie
authors.initials: S
authors.lastname: Juliant
authors.affiliation: CNRS UMR8576, Unité de Glycobiologie Structurale et Fonctionnelle, Université Lille Nord de France, Lille1, Villeneuve d'Ascq, France.
authors.forename: Anne
authors.initials: A
authors.lastname: Harduin-Lepers
authors.affiliation: CNRS UPS3044 Baculovirus et Thérapie, Saint Christol Lèz Alès, France.
authors.forename: François
authors.initials: F
authors.lastname: Monjaret
authors.affiliation: CNRS UMR8576, Unité de Glycobiologie Structurale et Fonctionnelle, Université Lille Nord de France, Lille1, Villeneuve d'Ascq, France; Laboratoire Français du Fractionnement et des Biotechnologies de Lille, Lille, France.
authors.forename: Béatrice
authors.initials: B
authors.lastname: Catieau
authors.affiliation: CNRS UPS3044 Baculovirus et Thérapie, Saint Christol Lèz Alès, France.
authors.forename: Marie-Luce
authors.initials: ML
authors.lastname: Violet
authors.affiliation: CNRS UPS3044 Baculovirus et Thérapie, Saint Christol Lèz Alès, France.
authors.forename: Pierre
authors.initials: P
authors.lastname: Cérutti
authors.affiliation: CNRS UPS3044 Baculovirus et Thérapie, Saint Christol Lèz Alès, France.
authors.forename: Annick
authors.initials: A
authors.lastname: Ozil
authors.affiliation: CNRS UPS3044 Baculovirus et Thérapie, Saint Christol Lèz Alès, France.
authors.forename: Martine
authors.initials: M
authors.lastname: Duonor-Cérutti
mesh_terms: D000818:Animals; D001483:Base Sequence; D005075:Biological Evolution; D003001:Cloning, Molecular; D005091:Exons; D005647:Fucosyltransferases / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D016678:Genome; D019476:Insect Proteins / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D007313:Insecta / Q000235:genetics; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010802:Phylogeny; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D061987:Sf9 Cells; D018411:Spodoptera / Q000235:genetics
chemical_list: D019476:Insect Proteins; D011994:Recombinant Proteins; D005647:Fucosyltransferases