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http://purl.uniprot.org/citations/18768906 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18768906 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18768906 | http://www.w3.org/2000/01/rdf-schema#comment | "We compare three Arabidopsis (Arabidopsis thaliana) complex glycan1 (cgl1) alleles and report on genetic interaction with staurosporin and temperature sensitive3a (stt3a). STT3a encodes a subunit of oligosaccharyltransferase that affects efficiency of N-glycan transfer to nascent secretory proteins in the endoplasmic reticulum; cgl1 mutants lack N-acetyl-glucosaminyltransferase I activity and are unable to form complex N-glycans in the Golgi apparatus. By studying CGL1-green fluorescent protein fusions in transient assays, we show that the extra N-glycosylation site created by a point mutation in cgl1 C5 is used in planta and interferes with folding of full-length membrane-anchored polypeptides in the endoplasmic reticulum. Tunicamycin treatment or expression in the stt3a-2 mutant relieved the folding block, and migration to Golgi stacks resumed. Complementation tests with C5-green fluorescent protein and other N-glycosylation variants of CGL1 demonstrated that suppression of aberrant N-glycosylation restores activity. Interestingly, CGL1 seems to be functional also as nonglycosylated enzyme. Two other cgl1 alleles showed splicing defects of their transcripts. In cgl1 C6, a point mutation affects the 3' splice site of intron 14, resulting in frame shifts; in cgl1-T, intron 11 fails to splice due to insertion of a T-DNA copy. Introgression of stt3a-2 did not restore complex glycan formation in cgl1 C6 or cgl1-T but suppressed the N-acetyl-glucosaminyltransferase I defect in cgl1 C5. Root growth assays revealed synergistic effects in double mutants cgl1 C6 stt3a-2 and cgl1-T stt3a-2 only. Besides demonstrating the conditional nature of cgl1 C5 in planta, our observations with loss-of-function alleles cgl1 C6 and cgl1-T in the stt3a-2 underglycosylation background prove that correct N-glycosylation is important for normal root growth and morphology in Arabidopsis."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.org/dc/terms/identifier | "doi:10.1104/pp.108.127027"xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.org/dc/terms/identifier | "doi:10.1104/pp.108.127027"xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Frank J."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Frank J."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Rips S."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Rips S."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "von Schaewen A."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "von Schaewen A."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Koiwa H."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Koiwa H."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Kaulfuerst-Soboll H."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/author | "Kaulfuerst-Soboll H."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/name | "Plant Physiol."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/name | "Plant Physiol."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/pages | "1354-1367"xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/pages | "1354-1367"xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/title | "Comparative analyses of arabidopsis complex glycan1 mutants and genetic interaction with staurosporin and temperature sensitive3a."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/title | "Comparative analyses of arabidopsis complex glycan1 mutants and genetic interaction with staurosporin and temperature sensitive3a."xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/volume | "148"xsd:string |
http://purl.uniprot.org/citations/18768906 | http://purl.uniprot.org/core/volume | "148"xsd:string |