2017 Fiscal Year Final Research Report
A new regulatory mechanism of the yeast amino acid permease by phosphorylation
| Project/Area Number |
16H07162
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| Research Category |
Grant-in-Aid for Research Activity Start-up
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied microbiology
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| Research Institution | Aoyama Gakuin University |
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Principal Investigator |
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| Project Period (FY) |
2016-08-26 – 2018-03-31
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| Keywords | アミノ酸輸送体 / リン酸化 / 出芽酵母 / アレスチン様タンパク質 |
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| Outline of Final Research Achievements |
It is known that defects in availability of tryptophan, one of the essential amino acids, cause Hartnup disorder and failure to thrive in childhood. Therefore, exploration of the mechanism of the diseases is important from the medical perspectives. This study aimed at basic understandings of the regulation of tryptophan permease in the yeast Saccharomyces cerevisiae. We examined whether degradation of the low-affinity tryptophan permease Tat1 depended on its phosphorylation. Mutants with altered phosphorylation activities were used to analyze the degradation of Tat1. We suggested that a casein kinase mediated phosphorylation of Tat1, and phosphorylation occurred at the N-terminal cytoplasmic domain of Tat1.
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| Free Research Field |
分子遺伝学
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