Identification of methylated GnTI-dependent N-glycans in Botryococcus brauni

In contrast to mammals and vascular plants, microalgae show a high diversity in the N-glycan structures of complex N-glycoproteins. Although homologues for β1,2-N-acetylglucosaminyltransferase I (GnTI), a key enzyme in the formation of complex N-glycans, have been identified in several algal species, GnTI-dependent N-glycans have not been detected so far. We have performed an N-glycoproteomic analysis of the hydrocarbon oils accumulating green microalgae Botryococcus braunii. Thereby, the analysis of intact N-glycopeptides allowed the determination of N-glycan compositions. Furthermore, insights into the role of N-glycosylation in B. braunii were gained from functional annotation of the identified N-glycoproteins. In total, 517 unique N-glycosylated peptides have been identified, including intact N-glycopeptides that harbored N-acetylhexosamine (HexNAc) at the nonreducing end. Surprisingly, these GnTI-dependent N-glycans were also found to be modified with (di)methylated hexose. The identification of GnTI-dependent N-glycans in combination with N-glycan methylation in B. braunii revealed an uncommon type of N-glycan processing in this microalgae.

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Bibliographic Details
Main Authors: Schulze, Stefan, Urzica, Eugen, Reijnders, Maarten J.M.F., van de Geest, Henri, Warris, Sven, Bakker, Linda V., Fufezan, Christian, Martins dos Santos, Vitor A.P., Schaap, Peter J., Peters, Sander A., Hippler, Michael
Format: Article/Letter to editor biblioteca
Language:English
Subjects:Botryococcus braunii, N-glycosylation, gene ontology annotation, mass spectrometry, post-translational modification,
Online Access:https://research.wur.nl/en/publications/identification-of-methylated-gnti-dependent-n-glycans-in-botryoco
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