Supplemental Data
Files in this Data Supplement:
- Supplemental Figure 1 - Peptides attached to the porous graphitic carbon (PGC) column and in the flow through were analyzed. Most of the peptides were observed in the bound fraction.
- Supplemental Figure 2 - Venn diagram of the proteins without a signal peptide identified through shotgun sequencing after MLAC.
- Supplemental Figure 3 - Comparison between glycoproteins identified in the present study and those from previous studies in plants. Previous studies used Arabidopsis as biological system, so Arabidopsis homologs of tomato glycoproteins were used for the comparison.
- Supplemental Figure 4 - Specific location of the N-glycosylation sites in the protein sequence of the xyloglucan-specific endoglucanase inhibitor protein (XEGIP).
- Supplemental Data 1 - MS/MS spectra of identified N-glycopeptides. The symbol nomenclature for glycan representation was followed according to Varki et al. (2009).
- Supplemental Data 2 - MS/MS spectra of the N-glycans of the recombinant xyloglucan-specific endoglucanase inhibitor protein (XEGIP).
- Supplemental figure legends - Supplemental figure legends
- Supplemental Table S1 - Proteins identified in the N-glycoproteome of tomato fruit, using a shotgun approach.
- Supplemental Table S2 - Glycopeptides identified following PGNase A treatment. Deamination was considered in peptides that contain the sequon N- X- S/T and peptides from proteins with a predicted SP.
- Supplemental Table S3 - Analysis of the predicted physicochemical properties of N-glycopeptides, identified after treatment with PNGase A.
- Supplemental Table S4 - Total proteins identified using shotgun proteomics and after the treatment with PNGase A. Protein homologs from Arabidopsis were used to search the tomato database.
- Supplemental Table S5 - Proposed subcellular location of identified glycoproteins based on bioinformatic analysis.
- Supplemental Table S6 - Proteins without predicted signal peptide identified through shotgun proteomics after MLAC.