FN Archimer Export Format
PT J
TI N-Glycans of Phaeodactylum tricornutum Diatom and Functional Characterization of Its N-Acetylglucosaminyltransferase I Enzyme
BT 
AF 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
AS 1:1;2:1;3:2;4:1;5:1;6:1;7:1;8:3;9:3;10:2;11:2;12:1;13:1;
FF 1:;2:;3:PDG-RBE-BRM-PBA;4:;5:;6:;7:;8:;9:;10:PDG-RBE-BRM-PBA;11:PDG-RBE-BRM-PBA;12:;13:;
C1 Univ Rouen, Lab Glycobiol & Matrice Extracellulaire Vegetale, Fac Sci, F-76821 Mont St Aignan, France.
   Ctr Nantes, Inst Francais Rech Exploitat Mer, Lab Physiol & Biotechnol Algues, F-44311 Nantes 03, France.
   Univ Rouen, INSERM, Lab Differenciat & Commun Neuronale & Neuroendocr, Fac Sci,U982,IFRM23, F-76821 Mont St Aignan, France.
C2 UNIV ROUEN, FRANCE
   IFREMER, FRANCE
   UNIV ROUEN, FRANCE
SI NANTES
SE PDG-RBE-BRM-PBA
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 4.773
TC 47
UR https://archimer.ifremer.fr/doc/00031/14184/11951.pdf
LA English
DT Article
AB 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.
PY 2011
PD FEB
SO Journal Of Biological Chemistry
SN 0021-9258
PU Amer Soc Biochemistry Molecular Biology Inc
VL 286
IS 8
UT 000287476400024
BP 6152
EP 6164
DI 10.1074/jbc.M110.175711
ID 14184
ER

EF