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http://purl.uniprot.org/citations/22492205http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22492205http://www.w3.org/2000/01/rdf-schema#comment"Rot1 is an essential yeast protein originally shown to be implicated in such diverse processes such as β-1,6-glucan synthesis, actin cytoskeleton dynamics or lysis of autophagic bodies. More recently also a role as a molecular chaperone has been discovered. Here, we report that Rot1 interacts in a synthetic manner with Ost3, one of the nine subunits of the oligosaccharyltransferase (OST) complex, the key enzyme of N-glycosylation. The deletion of OST3 in the rot1-1 mutant causes a temperature sensitive phenotype as well as sensitivity toward compounds interfering with cell wall biogenesis such as Calcofluor White, caffeine, Congo Red and hygromycin B, whereas the deletion of OST6, a functional homolog of OST3, has no effect. OST activity in vitro determined in membranes from rot1-1ost3Δ cells was found to be decreased to 45% compared with wild-type membranes, and model glycoproteins of N-glycosylation, like carboxypeptidase Y, Gas1 or dipeptidyl aminopeptidase B, displayed an underglycosylation pattern. By affinity chromatography, a physical interaction between Rot1 and Ost3 was demonstrated. Moreover, Rot1 was found to be involved also in the O-mannosylation process, as the glycosylation of distinct glycoproteins of this type were affected as well. Altogether, the data extend the role of Rot1 as a chaperone required to ensure proper glycosylation."xsd:string
http://purl.uniprot.org/citations/22492205http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cws068"xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/author"Lehle L."xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/author"Palamarczyk G."xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/author"Pasikowska M."xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/name"Glycobiology"xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/pages"939-947"xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/title"The essential endoplasmic reticulum chaperone Rot1 is required for protein N- and O-glycosylation in yeast."xsd:string
http://purl.uniprot.org/citations/22492205http://purl.uniprot.org/core/volume"22"xsd:string
http://purl.uniprot.org/citations/22492205http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22492205
http://purl.uniprot.org/citations/22492205http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22492205
http://purl.uniprot.org/uniprot/P48439#attribution-76AA913153D70377D634A39C32264E7Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/Q03691#attribution-76AA913153D70377D634A39C32264E7Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/#_A0A8H4BYS2-mappedCitation-22492205http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/#_Q03691-mappedCitation-22492205http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/#_P48439-mappedCitation-22492205http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/P48439http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/A0A8H4BYS2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22492205
http://purl.uniprot.org/uniprot/Q03691http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/22492205