| Registro completo |
| Provedor de dados: |
ArchiMer
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| País: |
France
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| Título: |
N-Glycans of Phaeodactylum tricornutum Diatom and Functional Characterization of Its N-Acetylglucosaminyltransferase I Enzyme
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| 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
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| Data: |
2011-02
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| Ano: |
2011
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| 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.
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| Tipo: |
Text
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| Idioma: |
Inglês
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| Identificador: |
http://archimer.ifremer.fr/doc/00031/14184/11951.pdf
DOI:10.1074/jbc.M110.175711
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| Editor: |
Amer Soc Biochemistry Molecular Biology Inc
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| Relação: |
http://archimer.ifremer.fr/doc/00031/14184/
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| Formato: |
application/pdf
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| Fonte: |
Journal Of Biological Chemistry (0021-9258) (Amer Soc Biochemistry Molecular Biology Inc), 2011-02 , Vol. 286 , N. 8 , P. 6152-6164
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| Direitos: |
2011 by The American Society for Biochemistry and Molecular Biology, Inc.
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