Protein N-glycosylation is similar in the moss Physcomitrella patens and in higher plants |
| |
Authors: | Viëtor Remco Loutelier-Bourhis Corinne Fitchette Anne-Catherine Margerie Pierre Gonneau Martine Faye Loïc Lerouge Patrice |
| |
Institution: | (1) CNRS–UMR 6037, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cedex, France;(2) CNRS–UMR 6014, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cedex, France;(3) ECODIV, Université de Rouen, 76821 Mont Saint Aignan Cedex, France;(4) Laboratoire de Biologie Cellulaire, INRA, Route de Saint Cyr, 78026 Versailles Cedex, France |
| |
Abstract: | We have investigated the structure of glycans N-linked to the proteins of the moss Physcomitrella patens. The structural elucidation was carried out by western blotting using antibodies specific for N-glycan epitopes and by analysis of N-linked glycans enzymatically released from a total protein extract by combination of MALDI–TOF and MALDI–PSD mass spectrometry analysis. Nineteen N-linked oligosaccharides were characterised ranging from high-mannose-type and truncated paucimannosidic-type to complex-type N-glycans harbouring core-xylose, core- (1,3)-fucose and Lewisa, as previously described for proteins from higher plants. This demonstrates that the processing of N-linked glycans, as well as the specificity of glycosidases and glycosyltransferases involved in this processing, are highly conserved between P. patens and higher plants. As a consequence, P. patens appears to be a new promising model organism for the investigation of the biological significance of protein N-glycosylation in the plant kingdom, taking advantage of the potential for gene targeting in this moss.Abbreviations Asn
asparagine
- CID
collision-induced dissociation
- Glc
glucose
- GlcNAc
N-acetylglucosamine
- Man
mannose
- MALDI–TOF MS
matrix-assisted laser desorption ionization–time of flight mass spectrometry
- PNGase A
peptide N-glycosidase A
- PSD
post-source decay |
| |
Keywords: | Physcomitrella N-Glycosylation Glycoprotein |
本文献已被 PubMed SpringerLink 等数据库收录! |
|