| http://purl.uniprot.org/citations/12441642 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12441642 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/12441642 | http://www.w3.org/2000/01/rdf-schema#comment | "MPC1/GPI13/YLL031C, one of the genes involved in the addition of phospho-ethanolamine to the glycosylphosphatidylinositol (GPI) anchor core, is an essential gene. Three available temperature-sensitive mutant alleles, mpc1-3, mpc1-4, and mpc1-5, displayed different phenotypes to each other and, correspondingly, these mutants were found to have different mutations in the MPC1 ORF. Temperature-sensitivity of mpc1-5 mutants was suppressed by 5 mM ZnSO(4) and by 5 mM MnCl(2). Multicopy suppressors were isolated from mpc1-5 mutant. Suppressors commonly effective to mpc1-4 and mpc1-5 mutations are PSD1, encoding phosphatidylserine decarboxylase, and ECM33, which were found to suppress the temperature-sensitive phenotype shown by the fsr2-1 and las21delta mutants, those of which have defects in the GPI anchor synthesis. PSD2, encoding another phosphatidylserine decarboxylase that is localized in Golgi/vacuole, was found to be able to serve as a multicopy suppressor of mpc1 and fsr2-1 mutants but not of the las21 delta mutant. In contrast to psd1delta, psd2delta showed a synthetic growth defect with mpc1 mutants but not with fsr2-1 or las21delta. Furthermore, psd1delta psd2delta mpc1 triple mutants did not form colonies on nutrient medium unless ethanolamine was supplied to the medium, whereas psd1delta psd2 delta fsr2-1 or psd1delta psd2 delta las21delta triple mutants grew on nutrient medium without supplementation of ethanolamine. These observations suggest that Mpc1 preferentially utilizes phosphatidylethanolamine produced by Psd2 that is localized in Golgi/vacuole. fsr2-1 dpl1 Delta psd1delta strains showed slower growth than fsr2-1 dpl1delta psd2 delta, suggesting that Fsr2 enzyme depends more on Dpl1 and Psd1 for production of phosphatidylethanolamine. Las21 did not show preference for the metabolic pathway to produce phosphatidylethanolamine."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.org/dc/terms/identifier | "doi:10.1266/ggs.77.309"xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.org/dc/terms/identifier | "doi:10.1266/ggs.77.309"xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/author | "Toh-e A."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/author | "Toh-e A."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/author | "Oguchi T."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/author | "Oguchi T."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/date | "2002"xsd:gYear |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/name | "Genes Genet. Syst."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/name | "Genes Genet. Syst."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/pages | "309-322"xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/pages | "309-322"xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/title | "Genetic characterization of genes encoding enzymes catalyzing addition of phospho-ethanolamine to the glycosylphosphatidylinositol anchor in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/title | "Genetic characterization of genes encoding enzymes catalyzing addition of phospho-ethanolamine to the glycosylphosphatidylinositol anchor in Saccharomyces cerevisiae."xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/volume | "77"xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://purl.uniprot.org/core/volume | "77"xsd:string |
| http://purl.uniprot.org/citations/12441642 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12441642 |
| http://purl.uniprot.org/citations/12441642 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/12441642 |
| http://purl.uniprot.org/citations/12441642 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12441642 |
| http://purl.uniprot.org/citations/12441642 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/12441642 |
| http://purl.uniprot.org/uniprot/Q07830 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/12441642 |
| http://purl.uniprot.org/uniprot/Q07830#attribution-0D4BD75BCE6E7F9ACA9F0B20889EFCC5 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/12441642 |