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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 Man 5 GlcNAc 2  intermediate. In contrast, glycans  N- linked to  Chlamydomonas reinhardtii  proteins arise from a GnTI-independent Golgi processing of oligomannosides giving rise to Man 5 GlcNAc 2  substituted eventually with one or two xylose(s). Here, complementation of  C. reinhardtii  with heterologous GnTI was investigated by expression of GnTI cDNAs originated from Arabidopsis and the diatom  Phaeodactylum tricornutum . No modification of the  N- glycans was observed in the GnTI transformed cells. Consequently, the structure of the Man 5 GlcNAc 2  synthesized by  C. reinhardtii  was reinvestigated. Mass spectrometry analyses combined with enzyme sequencing showed that  C. reinhardtii  proteins carry linear Man 5 GlcNAc 2  instead of the branched structure usually found in eukaryotes. Moreover, characterization of the lipid-linked oligosaccharide precursor demonstrated that  C. reinhardtii  exhibit a Glc 3 Man 5 GlcNAc 2  dolichol pyrophosphate precursor. We propose that this precursor is then trimmed into a linear Man 5 GlcNAc 2  that is not substrate for GnTI. Furthermore, cells expressing GnTI exhibited 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.

scientific reports

Heterologous expression of the N-acetylglucosaminyltransferase I dictates a reinvestigation of the N-glycosylation pathway in Chlamydomonas reinhardtii