Proteomics

Dataset Information

N-Glycoproteomic Analysis of Botryococcus Braunii

ABSTRACT: We have performed an N-glycoproteomic analysis of the green microalgae Botryococcus braunii, a promising candidate for the production of biofuels, accumulating considerable amounts of hydrocarbon oils. Thereby, three different strains have been compared: Showa (Race B), AC761 (Race B) and CCALA778 (Race A) which differ in the type of produced hydrocarbons. In total, 517 unique N-glycosylated peptides have been identified analyzing intact N-glycopeptides as well as deglycosylated, 18O-labeled peptides. Intact N-glycopeptides that harbored N-acetylhexosamine (HexNAc) at the non-reducing end were identified. Surprisingly, these GnTI-dependent N-glycans were also found to be modified with (di)methylated hexose. This type of methylated GnTI-dependent N-glycans has not been described so far.

INSTRUMENT(S):

ORGANISM(S): Botryococcus Braunii

TISSUE(S): Photosynthetic Cell

SUBMITTER: Stefan Schulze  

LAB HEAD: Michael Hippler

PROVIDER: PXD005708 | Pride | 2017-08-08

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
AC761_20160205_proteins_target_decoy.fasta Fasta
CCALA778_proteins_target_decoy.fasta Fasta
Glyco_all_18O_results_merged.csv Csv
Glyco_all_18O_results_merged.u.json.u.json Other
Glyco_all_ISCID_results_N-HexNAc_merged.csv Csv
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