ZFIN ID: ZDB-PUB-150715-22
Molecular phylogeny and functional genomics of beta-galactoside alpha2,6-sialyltransferases that explain ubiquitous expression of st6gal1 gene in amniotes
Petit, D., Mir, A., Petit, J., Thisse, C., Delannoy, P., Oriol, R., Thisse, B., Harduin-Lepers, A.
Date: 2010
Source: The Journal of biological chemistry   285: 38399-38414 (Journal)
Registered Authors: Thisse, Bernard, Thisse, Christine
Keywords: Evolution, Gene expression, Glycolipids, Glycoprotein biosynthesis, Glycosylation, Sialytransferases, Sialic acid
MeSH Terms:
  • Animals
  • Antigens, CD/genetics*
  • Evolution, Molecular*
  • Genome, Human*
  • Humans
  • Phylogeny*
  • Sequence Analysis, Protein
  • Sialyltransferases/genetics*
PubMed: 20855889 Full text @ J. Biol. Chem.
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.