Capítulo de Libro
A practical approach to reconstruct evolutionary history of animal sialyltransferases and gain insights into the sequence-function relationships of Golgi-glycosyltransferases
Título del libro: Glycosyltransferases : Methods and Protocols
Petit, Daniel; Teppa, Roxana Elin
; Petit, Jean Michel; Harduin Lepers, Anne
![Icon](/themes/CONICETDigital/images/conicet.png)
Otros responsables:
Brockhausen, Inka
Fecha de publicación:
2013
Editorial:
Humana Press
ISBN:
978-1-62703-464-7
Idioma:
Inglés
Clasificación temática:
Resumen
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.
Palabras clave:
SIALYLTRANSFERASES
,
MOLECULAR PHYLOGENY
,
PHYLOGENOMICS
,
GLYCOSILATION
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Capítulos de libros de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Capítulos de libros de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Citación
Petit, Daniel; Teppa, Roxana Elin; Petit, Jean Michel; Harduin Lepers, Anne; A practical approach to reconstruct evolutionary history of animal sialyltransferases and gain insights into the sequence-function relationships of Golgi-glycosyltransferases; Humana Press; 1022; 2013; 73-97
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