A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases.

Zoran Minic , Elisabeth Jamet (1) , Luc Négroni (2) , P. Arsene Der Garabedian (3) , Michel Zivy (2) , Lise Jouanin

1 SCSV - Surfaces Cellulaires et Signalisation chez les Végétaux
2 GQE-Le Moulon - Génétique Quantitative et Evolution - Le Moulon (Génétique Végétale)
3 Laboratoire d'Enzymologie des Acides Nucléiques

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.

Keywords: Arabidopsis thaliana; cell wall; concanavalin A; glycoside hydrolase; glycosylation; plant stem

Domains: Genomics [q-bio.GN]

Zoran Minic, Elisabeth Jamet, Luc Négroni, P. Arsene Der Garabedian, Michel Zivy, et al.. A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases.. Journal of Experimental Botany, 2007, 58 (10), pp.1. ⟨10.1093/jxb/erm082⟩. ⟨hal-00154429⟩