Abstract
In higher vertebrates, sialyltransferases catalyze the transfer of sialic acid residues, either Neu5Ac or Neu5Gc or KDN from an activated sugar donor, which is mainly CMP-Neu5Ac in human tissues, to the hydroxyl group of another saccharide acceptor. In the human genome, 20 unique genes have been described that encode enzymes with remarkable specificity with regards to their acceptor substrates and the glycosidic linkage formed. A systematic search of sialyltransferase-related sequences in genome and EST databases and the use of bioinformatic tools enabled us to investigate the evolutionary history of animal sialyltransferases and propose original models of divergent evolution of animal sialyltransferases. In this chapter, we extend our phylogenetic studies to the comparative analysis of the environment of sialyltransferase gene loci (synteny and paralogy studies), the variations of tissue expression of these genes and the analysis of amino-acid position evolution after gene duplications, in order to assess their sequence–function relationships and the molecular basis underlying their functional divergence.
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Acknowledgments
The project was financially supported by the University of Lille1 (ppf bioinformatique de Lille1), by the French Centre National de la Recherche Scientifique (CNRS), and by the Agence Nationale de la Recherche (ANR) project GalFish (ANR-2010-BLAN-120401). An Erasmus Mundus doctoral fellowship was attributed to R.E. Teppa.
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Petit, D., Teppa, R.E., Petit, JM., Harduin-Lepers, A. (2013). A Practical Approach to Reconstruct Evolutionary History of Animal Sialyltransferases and Gain Insights into the Sequence–Function Relationships of Golgi-Glycosyltransferases. In: Brockhausen, I. (eds) Glycosyltransferases. Methods in Molecular Biology, vol 1022. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-465-4_7
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