Abstract
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 (Asp144-->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 Asp144-->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 Asn144 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.
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Claims 5
Claim · model-written summary
Cloning of cgl GnTI cDNA revealed a point mutation causing an Asp144-->Asn substitution.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianat0 - Material
- cgle1
- Gene
- GnTIe1
- Outcome
- point mutatione1
- Qualifier
- critical amino acid substitutione1
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e1“Molecular cloning of cgl GnTI cDNA revealed a point mutation, which causes a critical amino acid substitution (Asp144-->Asn)”
Claim · model-written summary
Expression of cgl GnTI in insect cells confirmed a lack of enzyme activity.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Gene
- cgl GnTIe2
- Outcome
- lack of activitye2
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e2“Heterologous expression of cgl GnTI in insect cells confirmed its lack of activity and the use of the N-glycosylation site”
Claim · model-written summary
The Asp144-->Asn mutation in rabbit GnTI led to strongly reduced but still detectable enzymic activity.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Treatment
- introduction of the Asp144-->Asn mutation into rabbit GnTIe3
- Gene
- rabbit GnTIe3
- Outcome
- enzymic activitye3
- Direction
- strongly reducede3
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e3“introduction of the Asp144-->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”
Claim · model-written summary
Expression of Asn144 rabbit GnTI in cgl plants partially restored complex N-glycan formation.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Treatment
- Expression of Asn144 rabbit GnTIe4
- Outcome
- complex N-glycan formatione4
- Direction
- partially restoree4
- Comparator
- cgl plantse4
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e4“Expression of Asn144 rabbit GnTI in cgl plants could partially restore complex N-glycan formation”
Claim · model-written summary
The complete deficiency of GnTI activity in cgl plants is mainly due to the additional N-glycan, which may interfere with enzyme folding.
- Taxon
- Arabidopsis thalianaArabidopsis thalianat0
- Outcome
- complete deficiency of GnTI activitye5
- Qualifier
- additional N-glycane5
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e5“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”
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