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PMID:17526915
Citation |
Minic, Z, Jamet, E, Négroni, L, Arsene der Garabedian, P, Zivy, M and Jouanin, L (2007) A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases. J. Exp. Bot. 58:2503-12 |
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Abstract |
N-glycosylated proteins were isolated from Arabidopsis thaliana mature stems using affinity chromatography on Concanavalin A Sepharose, separated by 2D-electrophoresis and identified using nanoHPLC-MS/MS and MALDI-TOF MS. 102 glycoproteins were identified. 94% of these proteins were predicted by bioinformatics to be targeted to the secretory pathway and 87% of them were predicted to be localized in the cell wall or at the plasma membrane. 30% of these proteins belong to glycoside hydrolase (GH) families with some of them possibly involved in the hydrolysis of cell wall polysaccharides. The second major class of identified proteins comprises aspartyl and serine proteases. Other proteins are predicted to be oxido-reductases, contain interacting domains, are potentially involved in signalling or have an unknown function. This is, to our knowledge, the first survey of plant cell wall N-glycosylated proteins. |
Links |
PubMed PMC2394711 Online version:10.1093/jxb/erm082 |
Keywords |
Arabidopsis/enzymology; Arabidopsis/growth & development; Arabidopsis Proteins/classification; Arabidopsis Proteins/metabolism; Arabidopsis Proteins/physiology; Cell Wall/enzymology; Chromatography, Affinity/methods; Chromatography, High Pressure Liquid; Computational Biology; Concanavalin A/chemistry; Glycoside Hydrolases/metabolism; Glycoside Hydrolases/physiology; Glycosylation; Plant Stems/enzymology; Plant Stems/growth & development; Proteome; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
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Significance
Annotations
Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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