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-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.
journal_name
Plantajournal_title
Plantaauthors
Viëtor R,Loutelier-Bourhis C,Fitchette AC,Margerie P,Gonneau M,Faye L,Lerouge Pdoi
10.1007/s00425-003-1099-zsubject
Has Abstractpub_date
2003-12-01 00:00:00pages
269-75issue
2eissn
0032-0935issn
1432-2048journal_volume
218pub_type
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