Molecular phylogeny and functional genomics of beta-galactoside alpha2,6-sialyltransferases that explain ubiquitous expression of st6gal1 gene in amniotes.
Sialyltransferases are key enzymes in the biosynthesis of sialoglycoconjugates that catalyze the transfer of sialic residue from its activated form to an oligosaccharidic acceptor. β-Galactoside α2,6-sialyltransferases ST6Gal I and ST6Gal II are the two unique members of the ST6Gal family described in higher vertebrates. The availability of genome sequences enabled the identification of more distantly related invertebrates' st6gal gene sequences and allowed us to propose a scenario of their evolution. Using a phylogenomic approach, we present further evidence of an accelerated evolution of the st6gal1 genes both in their genomic regulatory sequences and in their coding sequence in reptiles, birds, and mammals known as amniotes, whereas st6gal2 genes conserve an ancestral profile of expression throughout vertebrate evolution.
Petit
Daniel
D
Unité de Génétique Moléculaire Animale, Université de Limoges Faculté des Sciences et Techniques, INRA UMR 1061, 123 Avenue Albert Thomas, 87060 Limoges, France.
Mir
Anne-Marie
AM
Petit
Jean-Michel
JM
Thisse
Christine
C
Delannoy
Philippe
P
Oriol
Rafael
R
Thisse
Bernard
B
Harduin-Lepers
Anne
A
D000818:Animals; D015703:Antigens, CD / Q000235:genetics*; D019143:Evolution, Molecular; D015894:Genome, Human; D006801:Humans; D010802:Phylogeny; D020539:Sequence Analysis, Protein; D012799:Sialyltransferases / Q000235:genetics*; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase
D015703:Antigens, CD; D012799:Sialyltransferases; C093493:ST6GAL1 protein, human; D000094802:beta-D-Galactoside alpha 2-6-Sialyltransferase; C549032:ST6GAL2 protein, human