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Characterization of N-Glycans from Arabidopsis. Application to a Fucose-Deficient Mutant1

Catherine Rayon, Marion Cabanes-Macheteau, Corinne Loutelier-Bourhis, Isabelle Salliot-Maire, Jérome Lemoine, Wolf-Dieter Reiter, Patrice Lerouge, and Loïc Faye*

Laboratoire des Transports Intracellulaires, Centre National de la Recherche Scientifique (CNRS)-ESA 6037 (C.R., M.C.-M., P.L., L.F.), Spectroscopie de Masse Bioorganique (C.L.-B.), and Laboratoire de Résonance Magnétique Nucléaire, CNRS-ESA 6014 (I.S.-M.), IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan, France; IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan, FranceLaboratoire de Chimie Biologique, CNRS-Unite, Mixte de Recherche 111, Université de Lille, 59655 Villeneuve d'Ascq, France (J.L.); and Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut 06269 (W.-D.R.)

The structures of glycans N-linked to Arabidopsis proteins have been fully identified. From immuno- and affinodetections on blots, chromatography, nuclear magnetic resonance, and glycosidase sequencing data, we show that Arabidopsis proteins are N-glycosylated by high-mannose-type N-glycans from Man5GlcNAc2 to Man9GlcNAc2, and by xylose- and fucose (Fuc)-containing oligosaccharides. However, complex biantenary structures containing the terminal Lewis a epitope recently reported in the literature (A.-C. Fitchette-Lainé, V. Gomord, M. Cabanes, J.-C. Michalski, M. Saint Macary, B. Foucher, B. Cavalier, C. Hawes, P. Lerouge, and L. Faye [1997] Plant J 12: 1411-1417) were not detected. A similar study was done on the Arabidopsis mur1 mutant, which is affected in the biosynthesis of L-Fuc. In this mutant, one-third of the Fuc residues of the xyloglucan has been reported to be replaced by L-galactose (Gal) (E. Zablackis, W.S. York, M. Pauly, S. Hantus, W.D. Reiter, C.C.S. Chapple, P. Albersheim, and A. Darvill [1996] Science 272: 1808-1810). N-linked glycans from the mutant were identified and their structures were compared with those isolated from the wild-type plants. In about 95% of all N-linked glycans from the mur1 plant, L-Fuc residues were absent and were not replaced by another monosaccharide. However, in the remaining 5%, L-Fuc was found to be replaced by a hexose residue. From nuclear magnetic resonance and mass spectrometry data of the mur1 N-glycans, and by analogy with data reported on mur1 xyloglucan, this subpopulation of N-linked glycans was proposed to be L-Gal-containing N-glycans resulting from the replacement of L-Fuc by L-Gal.

1   This work was supported in France by CNRS (no. ESA 6037), the University of Rouen, and the M.E.N.E.S.R. (Actions Concertées Coordonnées des Sciences du Vivant ACCSV 14, réseau G-Trec), and by grants from the Région Haute-Normandie. This work was supported in the United States by the Department of Energy Biosciences Program (grant no. DE-FG02-95ER20203). C.R. and M.C.-M. are recipients of Region Haute-Normandie and Biopole fellowships, respectively.
*   Corresponding author; e-mail lfaye{at}crihan.fr; fax 33-2-35-14-67-87.

Plant Physiol. (1999) 119: 725-734
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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