Titre :

Rhamnogalacturonan II structure shows variation in the side chains monosaccharide composition and methylation status within and across different plant species

Auteur(s) :

Pabst, Martin [Auteur]

Fischl, Richard M. [Auteur]

Brecker, Lothar [Auteur]

Morelle, Willy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Fauland, Alexander [Auteur]
Technische Universität Graz [TU Graz]
Köfeler, Harald [Auteur]

Altmann, Friedrich [Auteur]

Leonard, Renaud [Auteur]

Titre de la revue :

The Plant Journal. For Cell and Molecular Biology

Nom court de la revue :

Plant J.

Numéro :

76

Pagination :

61-72

Date de publication :

2013-10

ISSN :

1365-313X

Mot(s)-clé(s) en anglais :

Arabidopsis
Plant Leaves
porous graphitic carbon
Hexuronic Acids
Organ Specificity
Monosaccharides
Cell Wall
Arabidopsis thaliana
rhamnogalacturonan II
Spectrometry, Mass, Electrospray Ionization
structural analysis
PGCC-ESI-MS
Chromatography, Liquid
Mutation
Galactose
Pectins
plant cell wall
Fucose

Discipline(s) HAL :

Chimie/Chimie théorique et/ou physique

Résumé en anglais : [en]

A paradigm regarding rhamnogalacturonans II (RGII) is their strictly conserved structure within a given plant. We developed and employed a fast structural characterization method based on chromatography and mass spectrometry, ...
Lire la suite >A paradigm regarding rhamnogalacturonans II (RGII) is their strictly conserved structure within a given plant. We developed and employed a fast structural characterization method based on chromatography and mass spectrometry, allowing analysis of RGII side chains from microgram amounts of cell wall. We found that RGII structures are much more diverse than so far described. In chain A of wild-type plants, up to 45% of the l-fucose is substituted by l-galactose, a state that is seemingly uncorrelated with RGII dimerization capacity. This led us to completely reinvestigate RGII structures of the Arabidopsis thaliana fucose-deficient mutant mur1, which provided insights into RGII chain A biosynthesis, and suggested that chain A truncation, rather than l-fucose to l-galactose substitution, is responsible for the mur1 dwarf phenotype. Mass spectrometry data for chain A coupled with NMR analysis revealed a high degree of methyl esterification of its glucuronic acid, providing a plausible explanation for the puzzling RGII antibody recognition. The β-galacturonic acid of chain A exhibits up to two methyl etherifications in an organ-specific manner. Combined with variation in the length of side chain B, this gives rise to a family of RGII structures instead of the unique structure described up to now. These findings pave the way for studies on the physiological roles of modulation of RGII composition.Lire moins >

Langue :

Anglais

Audience :

Non spécifiée

Établissement(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Mécanismes moléculaires de la N-glycosylation et pathologies associées

Date de dépôt :

2020-02-12T15:12:08Z
2021-03-04T14:46:54Z