title: Evolutionary history of the alpha2,8-sialyltransferase (ST8Sia) gene family: tandem duplications in early deuterostomes explain most of the diversity found in the vertebrate ST8Sia genes.
abstract: BACKGROUND
  The animal sialyltransferases, which catalyze the transfer of sialic acid to the glycan moiety of glycoconjugates, are subdivided into four families: ST3Gal, ST6Gal, ST6GalNAc and ST8Sia, based on acceptor sugar specificity and glycosidic linkage formed. Despite low overall sequence identity between each sialyltransferase family, all sialyltransferases share four conserved peptide motifs (L, S, III and VS) that serve as hallmarks for the identification of the sialyltransferases. Currently, twenty subfamilies have been described in mammals and birds. Examples of the four sialyltransferase families have also been found in invertebrates. Focusing on the ST8Sia family, we investigated the origin of the three groups of alpha2,8-sialyltransferases demonstrated in vertebrates to carry out poly-, oligo- and mono-alpha2,8-sialylation.
  
  
  RESULTS
  We identified in the genome of invertebrate deuterostomes, orthologs to the common ancestor for each of the three vertebrate ST8Sia groups and a set of novel genes named ST8Sia EX, not found in vertebrates. All these ST8Sia sequences share a new conserved family-motif, named "C-term" that is involved in protein folding, via an intramolecular disulfide bridge. Interestingly, sequences from Branchiostoma floridae orthologous to the common ancestor of polysialyltransferases possess a polysialyltransferase domain (PSTD) and those orthologous to the common ancestor of oligosialyltransferases possess a new ST8Sia III-specific motif similar to the PSTD. In osteichthyans, we have identified two new subfamilies. In addition, we describe the expression profile of ST8Sia genes in Danio rerio.
  
  
  CONCLUSIONS
  Polysialylation appeared early in the deuterostome lineage. The recent release of several deuterostome genome databases and paralogons combined with synteny analysis allowed us to obtain insight into events at the gene level that led to the diversification of the ST8Sia genes, with their corresponding enzymatic activities, in both invertebrates and vertebrates. The initial expansion and subsequent divergence of the ST8Sia genes resulted as a consequence of a series of ancient duplications and translocations in the invertebrate genome long before the emergence of vertebrates. A second subset of ST8sia genes in the vertebrate genome arose from whole genome duplication (WGD) R1 and R2. Subsequent selective ST8Sia gene loss is responsible for the characteristic ST8Sia gene expression pattern observed today in individual species.
authors.affiliation: Laboratoire de Glycobiologie Structurale et Fonctionnelle, CNRS, UMR 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq, France. anne.harduin@univ-lille1.fr
authors.forename: Anne
authors.initials: A
authors.lastname: Harduin-Lepers
authors.forename: Daniel
authors.initials: D
authors.lastname: Petit
authors.forename: Rosella
authors.initials: R
authors.lastname: Mollicone
authors.forename: Philippe
authors.initials: P
authors.lastname: Delannoy
authors.forename: Jean-Michel
authors.initials: JM
authors.lastname: Petit
authors.forename: Rafael
authors.initials: R
authors.lastname: Oriol
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D030561:Databases, Nucleic Acid; D019143:Evolution, Molecular; D020440:Gene Duplication; D006801:Humans; D016013:Likelihood Functions; D016014:Linear Models; D051379:Mice; D005810:Multigene Family; D010802:Phylogeny; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012799:Sialyltransferases / Q000235:genetics*; D014714:Vertebrates / Q000235:genetics*; D015027:Zebrafish / Q000235:genetics
chemical_list: D012799:Sialyltransferases