Data/hora: 18/06/2024 03:16:47

Provedor de dados: 	5	
País: 	France	
Título: 	N-Glycans of Phaeodactylum tricornutum Diatom and Functional Characterization of Its N-Acetylglucosaminyltransferase I Enzyme	
Autores: 	Baiet, Berengere; Burel, Carole; Saint-jean, Bruno; Louvet, Romain; Menu-bouaouiche, Laurence; Kiefer-meyer, Marie-christine; Mathieu-rivet, Elodie; Lefebvre, Thomas; Castel, Helene; Carlier, Aude; Cadoret, Jean-paul; Lerouge, Patrice; Bardor, Muriel.	
Data: 	2011-02	
Ano: 	2011	
Resumo: 	N-Glycosylation, a major co- and post-translational event in the synthesis of proteins in eukaryotes, is unknown in aquatic photosynthetic microalgae. In this paper, we describe the N-glycosylation pathway in the diatom Phaeodactylum tricornutum. Bio-informatic analysis of its genome revealed the presence of a complete set of sequences potentially encoding for proteins involved in the synthesis of the lipid-linked Glc(3)Man(9)GlcNAc(2)-PP-dolichol N-glycan, some subunits of the oligosaccharyltransferase complex, as well as endoplasmic reticulum glucosidases and chaperones required for protein quality control and, finally, the alpha-mannosidase I involved in the trimming of the N-glycan precursor into Man-5 N-glycan. Moreover, one N-acetylglucosaminyltransferase I, a Golgi glycosyltransferase that initiates the synthesis of complex type N-glycans, was predicted in the P. tricornutum genome. We demonstrated that this gene encodes for an active N-acetylglucosaminyltransferase I, which is able to restore complex type N-glycans maturation in the Chinese hamster ovary Lec1 mutant, defective in its endogeneous N-acetylglucosaminyltransferase I. Consistent with these data, the structural analyses of N-linked glycans demonstrated that P. tricornutum proteins carry mainly high mannose type N-glycans ranging from Man-5 to Man-9. Although representing a minor glycan population, paucimannose N-glycans were also detected, suggesting the occurrence of an N-acetylglucosaminyltransferase I-dependent maturation of N-glycans in this diatom.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	http://archimer.ifremer.fr/doc/00031/14184/11951.pdf

DOI:10.1074/jbc.M110.175711	
Editor: 	Amer Soc Biochemistry Molecular Biology Inc	
Relação: 	http://archimer.ifremer.fr/doc/00031/14184/	
Formato: 	application/pdf	
Fonte: 	Journal Of Biological Chemistry (0021-9258) (Amer Soc Biochemistry Molecular Biology Inc), 2011-02 , Vol. 286 , N. 8 , P. 6152-6164	
Fonte: 	2011 by The American Society for Biochemistry and Molecular Biology, Inc.