A practical approach to reconstruct evolutionary history of animal sialyltransferases and gain insights into the sequence-function relationships of Golgi-glycosyltransferases.
Methods Mol Biol
; 1022: 73-97, 2013.
Article
en En
| MEDLINE
| ID: mdl-23765655
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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Sialiltransferasas
/
Glicosiltransferasas
/
Aparato de Golgi
Tipo de estudio:
Prognostic_studies
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Methods Mol Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2013
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos