Protein N-glycosylation is similar in the moss Physcomitrella patens and in higher plants.
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-alpha(1,3)-fucose and Lewis(a), 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.
Viëtor
Remco
R
CNRS-UMR 6037, IFRMP 23, Université de Rouen, 76821 Mont Saint Aignan Cedex, France.
Loutelier-Bourhis
Corinne
C
Fitchette
Anne-Catherine
AC
Margerie
Pierre
P
Gonneau
Martine
M
Faye
Loïc
L
Lerouge
Patrice
P
D019068:Bryopsida / Q000378:metabolism*; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism; D006031:Glycosylation; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D011134:Polysaccharides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D011487:Protein Conformation; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006023:Glycoproteins; D010940:Plant Proteins; D011134:Polysaccharides