Identification of methylated GnTI-dependent N-glycans in Botryococcus brauni.
Identification of methylated GnTI-dependent N-glycans in Botryococcus brauni.
复制标题
DOI：
10.1111/nph.14713
复制
发表时间：
2017-07
期刊：
影响因子：
--
通讯作者：
S. Schulze;E. Urzica;M. Reijnders;H. van de Geest;S. Warris;Linda V. Bakker;C. Fufezan;V. M. D. Martins dos Santos;P. Schaap;S. Peters;M. Hippler
中科院分区：
文献类型：
--
作者：
S. Schulze;E. Urzica;M. Reijnders;H. van de Geest;S. Warris;Linda V. Bakker;C. Fufezan;V. M. D. Martins dos Santos;P. Schaap;S. Peters;M. Hippler
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.
