{"title":"线粒体天门冬氨酸氨基转移酶(maa1)失活导致球囊酵母发生谷氨酸需要的 glu1 突变。","authors":"Kenji Kitamura","doi":"10.17912/micropub.biology.001338","DOIUrl":null,"url":null,"abstract":"<p><p>Two genomic genes, which rescue ammonium assimilation defect in the glutamate-requiring <i>Schizosaccharomyces</i> <i>pombe glu1</i> mutant, were identified. The <i>maa1</i> , encoding a mitochondrial aspartate aminotransferase, is the causative gene of <i>glu1</i> mutation because an inseparable linkage between <i>maa1</i> and <i>glu1</i> on the chromosome, and also the <i>glu1</i> mutant strain has a nonsense mutation within the <i>maa1</i> coding region, which is responsible for its defective phenotype. The <i>yhm2</i> , a mitochondrial 2-oxoglutarate carrier, was also isolated as a weak multicopy suppressor gene. These findings reiterate the importance of the mitochondria in utilizing the amino acids for cellular nitrogen metabolism.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2024 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2024-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11536045/pdf/","citationCount":"0","resultStr":"{\"title\":\"Mitochondrial aspartate aminotransferase ( <i>maa1</i> ) inactivation causes glutamate-requiring <i>glu1</i> mutation in <i>Schizosaccharomyces</i> <i>pombe</i>.\",\"authors\":\"Kenji Kitamura\",\"doi\":\"10.17912/micropub.biology.001338\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Two genomic genes, which rescue ammonium assimilation defect in the glutamate-requiring <i>Schizosaccharomyces</i> <i>pombe glu1</i> mutant, were identified. The <i>maa1</i> , encoding a mitochondrial aspartate aminotransferase, is the causative gene of <i>glu1</i> mutation because an inseparable linkage between <i>maa1</i> and <i>glu1</i> on the chromosome, and also the <i>glu1</i> mutant strain has a nonsense mutation within the <i>maa1</i> coding region, which is responsible for its defective phenotype. The <i>yhm2</i> , a mitochondrial 2-oxoglutarate carrier, was also isolated as a weak multicopy suppressor gene. These findings reiterate the importance of the mitochondria in utilizing the amino acids for cellular nitrogen metabolism.</p>\",\"PeriodicalId\":74192,\"journal\":{\"name\":\"microPublication biology\",\"volume\":\"2024 \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2024-10-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11536045/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"microPublication biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.17912/micropub.biology.001338\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"microPublication biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17912/micropub.biology.001338","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
Two genomic genes, which rescue ammonium assimilation defect in the glutamate-requiring Schizosaccharomycespombe glu1 mutant, were identified. The maa1 , encoding a mitochondrial aspartate aminotransferase, is the causative gene of glu1 mutation because an inseparable linkage between maa1 and glu1 on the chromosome, and also the glu1 mutant strain has a nonsense mutation within the maa1 coding region, which is responsible for its defective phenotype. The yhm2 , a mitochondrial 2-oxoglutarate carrier, was also isolated as a weak multicopy suppressor gene. These findings reiterate the importance of the mitochondria in utilizing the amino acids for cellular nitrogen metabolism.