A Practical Approach to Reconstruct ...
Type de document :
Partie d'ouvrage: Chapitre
URL permanente :
Titre :
A Practical Approach to Reconstruct Evolutionary History of Animal Sialyltransferases and Gain Insights into the Sequence–Function Relationships of Golgi-Glycosyltransferases
Auteur(s) :
Petit, Daniel [Auteur]
Unité de Génétique Moléculaire Animale [UMR GMA]
Teppa, Roxana [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Petit, Jean-Michel [Auteur]
Unité de Génétique Moléculaire Animale [UMR GMA]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Unité de Génétique Moléculaire Animale [UMR GMA]
Teppa, Roxana [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Petit, Jean-Michel [Auteur]
Unité de Génétique Moléculaire Animale [UMR GMA]
Harduin Lepers, Anne [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Éditeur(s) ou directeur(s) scientifique(s) :
Brockhausen, Inka
Titre de l’ouvrage :
Glycosyltransferases : Methods and Protocols
Numéro :
1022
Titre du fascicule / de la collection :
Methods in Molecular Biology
Pagination :
73-97
Éditeur :
Humana Press
Lieu de publication :
Totowa, NJ
Date de publication :
2013
ISBN :
978-1-62703-464-7, 978-1-62703-465-4
ISSN :
1064-3745, 1940-6029
Mot(s)-clé(s) en anglais :
Sialyltransferases
Molecular phylogeny
Phylogenomics
Evolution
Golgi
Glycosylation
Cloning
Molecular phylogeny
Phylogenomics
Evolution
Golgi
Glycosylation
Cloning
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
Régulation de la glycosylation terminale
Date de dépôt :
2020-02-12T15:44:44Z
2021-04-22T12:51:07Z
2021-04-22T12:51:07Z