Mitochondrial aspartate aminotransferase ( maa1 ) inactivation causes glutamate-requiring glu1 mutation in Schizosaccharomyces pombe .
| Autor: | Kitamura K; Department of Gene Science, Natural Science Center for Basic Research and Development, Hiroshima University, Higashi-Hiroshima, Hiroshima, Japan.; Genome Biotechnology, Graduate School of Integrated Sciences for Life, Hiroshima University, Higashi-Hiroshima, Hiroshima, Japan. |
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| Jazyk: | angličtina |
| Zdroj: | MicroPublication biology [MicroPubl Biol] 2024 Oct 21; Vol. 2024. Date of Electronic Publication: 2024 Oct 21 (Print Publication: 2024). |
| DOI: | 10.17912/micropub.biology.001338 |
| Abstrakt: | Two genomic genes, which rescue ammonium assimilation defect in the glutamate-requiring Schizosaccharomyces pombe 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. Competing Interests: The authors declare that there are no conflicts of interest present. (Copyright: © 2024 by the authors.) |
| Databáze: | MEDLINE |
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