| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/2000/01/rdf-schema#comment | "The MPR1 gene, which is found in the Sigma1278b strain but is not present in the sequenced laboratory strain S288C, of the budding yeast Saccharomyces cerevisiae encodes a previously uncharacterized N-acetyltransferase that detoxifies the proline analogue azetidine-2-carboxylate (AZC). However, it is unlikely that AZC is a natural substrate of Mpr1 because AZC is found only in some plant species. In our search for the physiological function of Mpr1, we found that mpr1-disrupted cells were hypersensitive to oxidative stresses and contained increased levels of reactive oxygen species (ROS). In contrast, overexpression of MPR1 leads to an increase in cell viability and a decrease in ROS level after oxidative treatments. These results indicate that Mpr1 can reduce intracellular oxidation levels. Because put2-disrupted yeast cells lacking Delta(1)-pyrroline-5-carboxylate (P5C) dehydrogenase have increased ROS, we examined the role of Mpr1 in put2-disrupted strains. When grown on media containing urea and proline as the nitrogen source, put2-disrupted cells did not grow as well as WT cells and accumulated intracellular levels of P5C that were first detected in yeast cells and ROS. On the other hand, put2-disrupted cells that overexpressed MPR1 had considerably lower ROS levels. In vitro studies with bacterially expressed Mpr1 demonstrated that Mpr1 can acetylate P5C, or, more likely, its equilibrium compound glutamate-gamma-semialdehyde, at neutral pH. These results suggest that the proline catabolism intermediate P5C is toxic to yeast cells because of the formation of ROS, and Mpr1 regulates the ROS level under P5C-induced oxidative stress."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0403349101"xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0403349101"xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/author | "Nomura M."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/author | "Nomura M."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/author | "Takagi H."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/author | "Takagi H."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/pages | "12616-12621"xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/pages | "12616-12621"xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/title | "Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/title | "Role of the yeast acetyltransferase Mpr1 in oxidative stress: regulation of oxygen reactive species caused by a toxic proline catabolism intermediate."xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/volume | "101"xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://purl.uniprot.org/core/volume | "101"xsd:string |
| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15308773 |
| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15308773 |
| http://purl.uniprot.org/citations/15308773 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15308773 |
| http://purl.uniprot.org/citations/15308773 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15308773 |
| http://purl.uniprot.org/citations/15308773 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15308773 |