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Literature summary for 2.4.1.101 extracted from

  • Vanier, G.; Lucas, P.L.; Loutelier-Bourhis, C.; Vanier, J.; Plasson, C.; Walet-Balieu, M.L.; Tchi-Song, P.C.; Remy-Jouet, I.; Richard, V.; Bernard, S.; Driouich, A.; Afonso, C.; Lerouge, P.; Mathieu-Rivet, E.; Bardor, M.
    Heterologous expression of the N-acetylglucosaminyltransferase I dictates a reinvestigation of the N-glycosylation pathway in Chlamydomonas reinhardtii (2017), Sci. Rep., 7, 10156 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
recombinant nuclear expression of the enzyme sequences fused to a tag sequence encoding for a V5-epitope in Chlamydomonas reinhardtii Phaeodactylum tricornutum
recombinant nuclear expression of the enzyme sequences fused to a tag sequence encoding for a V5-epitope in Chlamydomonas reinhardtii Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
additional information eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate. In contrast, glycans N-linked to Chlamydomonas reinhardtii proteins arise from a GnTI-independent Golgi processing of oligomannosides giving rise to Man5GlcNAc2 substituted eventually with one or two xylose(s). Chlamydomonas reinhardtii proteins carry linear Man5GlcNAc2 instead of the branched structure usually found in eukaryotes. Moreover, characterization of the lipid-linked oligosaccharide precursor demonstrated that Chlamydomonas reinhardtii exhibit a Glc3Man5GlcNAc2 dolichol diphosphate precursor. This precursor is then trimmed into a linear Man5GlcNAc2 that is not substrate for GnTI. Expression of GnTI cDNAs originated from Arabidopsis and the diatom Phaeodactylum tricornutum cause no modification of the N-glycans in the GnTI transformed cells. Cells expressing GnTI exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus Phaeodactylum tricornutum
additional information eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate. In contrast, glycans N-linked to Chlamydomonas reinhardtii proteins arise from a GnTI-independent Golgi processing of oligomannosides giving rise to Man5GlcNAc2 substituted eventually with one or two xylose(s). Chlamydomonas reinhardtii proteins carry linear Man5GlcNAc2 instead of the branched structure usually found in eukaryotes. Moreover, characterization of the lipid-linked oligosaccharide precursor demonstrated that Chlamydomonas reinhardtii exhibit a Glc3Man5GlcNAc2 dolichol diphosphate precursor. This precursor is then trimmed into a linear Man5GlcNAc2 that is not substrate for GnTI. Expression of GnTI cDNAs originated from Arabidopsis and the diatom Phaeodactylum tricornutum cause no modification of the N-glycans in the GnTI transformed cells. Cells expressing GnTI exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi membrane
-
 Arabidopsis thaliana 139
-
membrane
-
 Phaeodactylum tricornutum 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ required Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] Phaeodactylum tricornutum
-
 UDP + Man5GlcNAc3-[protein]
-
 ?
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein] Arabidopsis thaliana
-
 UDP + Man5GlcNAc3-[protein]
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q9XGM8
-
-
Phaeodactylum tricornutum G0WVT5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
-
 Phaeodactylum tricornutum UDP + Man5GlcNAc3-[protein]
-
 ?
UDP-N-acetyl-alpha-D-glucosamine + Man5GlcNAc2-[protein]
-
 Arabidopsis thaliana UDP + Man5GlcNAc3-[protein]
-
 ?

Synonyms

Synonyms Comment Organism
AtGnTI
-
 Arabidopsis thaliana
GnTI
-
 Phaeodactylum tricornutum
GnTI
-
 Arabidopsis thaliana
N-acetylglucosaminyltransferase I
-
 Phaeodactylum tricornutum
N-acetylglucosaminyltransferase I
-
 Arabidopsis thaliana
PtGnTI
-
 Phaeodactylum tricornutum

General Information

General Information Comment Organism
malfunction enzyme-deficient Chlamydomonas reinhardtii cells expressing eukaryotic GnTI from Arabidopsis thaliana exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus Arabidopsis thaliana
malfunction enzyme-deficient Chlamydomonas reinhardtii cells expressing eukaryotic GnTI from Phaeodactylum tricornutum exhibit an altered phenotype with large vacuoles, increase of ROS production and accumulation of starch granules, suggesting the activation of stress responses likely due to the perturbation of the Golgi apparatus Phaeodactylum tricornutum
metabolism eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate Phaeodactylum tricornutum
metabolism eukaryotic N-glycosylation pathways are dependent of N-acetylglucosaminyltransferase I (GnTI), a key glycosyltransferase opening the door to the formation of complex-type N-glycans by transferring a N-acetylglucosamine residue onto the Man5GlcNAc2 intermediate Arabidopsis thaliana
physiological function AtGnTI (At4g38240) encodes for a Golgi enzyme that is responsible for the transfer of a terminal GlcNAc residue onto Man5GlcNAc2 N-glycan Arabidopsis thaliana
physiological function PtGnTI restores in vivo the biosynthesis of complex-type N-glycans in CHO Lec1 mutant that lacks endogenous GnTI activity Phaeodactylum tricornutum