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
|
Allocation Type | Single-year Grants |
Research Field |
Applied microbiology
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Research Institution | Aoyama Gakuin University |
Principal Investigator |
|
Project Period (FY) |
2016-08-26 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
Budget Amount *help |
¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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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 / Saccharomyces cerevisiae / 低親和性トリプトファン輸送体Tat1 |
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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Report
(3 results)
Research Products
(4 results)