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Strasser, R; Stadlmann, J; Svoboda, B; Altmann, F; Glössl, J; Mach, L.
(2005): Molecular basis of N-acetylglucosaminyltransferase I deficiency in Arabidopsis thaliana plants lacking complex N-glycans.
Biochem J. 2005; 387(Pt 2):385-391 FullText FullText_BOKU

GnTI (N-acetylglucosaminyltransferase I) is a Golgi-resident enzyme essential for the processing of high-mannose to hybrid and complex N-glycans. The Arabidopsis thaliana cgl mutant lacks GnTI activity and as a consequence accumulates oligomannosidic structures. Molecular cloning of cgl GnTI cDNA revealed a point mutation, which causes a critical amino acid substitution (Asp(144) -> Asn), thereby creating an additional N-glycosylation site. Heterologous expression of cgl GnTI in insect cells confirmed its lack of activity and the use of the N-glycosylation site. Remarkably, introduction of the Asp(144) -> Asn mutation into rabbit GnTI, which does not result in the formation of a new N-glycosylation site, led to a protein with strongly reduced, but still detectable enzymic activity. Expression of Asn(144) rabbit GnTI in cgl plants could partially restore complex N-glycan formation. These results indicate that the complete deficiency of GnTI activity in cgl plants is mainly due to the additional N-glycan, which appears to interfere with the proper folding of the enzyme.
Authors BOKU Wien:
Altmann Friedrich
Glößl Josef
Mach Lukas
Stadlmann Johannes
Strasser Richard
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Animals -
Arabidopsis - enzymology
Cell Line - enzymology
Molecular Sequence Data - enzymology
Mutation - enzymology
N-Acetylglucosaminyltransferases - genetics
Plant Leaves - metabolism
Plants, Genetically Modified - metabolism
Polysaccharides - metabolism
Rabbits - metabolism
Sequence Alignment - metabolism
Sequence Homology, Amino Acid - metabolism

Find related publications in this database (Keywords)
Arabidopsis thaliana
N-acetylglucosaminyltransferase I

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