Mechanism of leucine signaling of Thermus thermophilus
| Project/Area Number |
22780084
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
Applied biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
TOMITA Takeo 東京大学, 生物生産工学研究センター, 助教 (50447364)
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| Project Period (FY) |
2010 – 2011
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| Project Status |
Completed (Fiscal Year 2011)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2010: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 好熱菌 / グルタミン酸脱水素酵素 / アロステリック調節 / グローバル調節 / ロイシン / 遺伝子発現調節 |
|---|
| Research Abstract |
We revealed that glutamate dehydrogenase(GDH) from Thermus thermophilus formed hetero-hexameric structure consisted from homologous two subunits ; catalytic subunit(GdhB) and regulatory subunit(GdhB), and this complex was subject to allosteric activation by hydrophobic amino acids especially leucine. We succeeded to determine the crystal structure of GdhA/GdhB/Leu complex and revealed the allosteric mechanism of GDH. GDH2 from human(hGDH2) is also subject to allosteric activation by leucine and we found that important residues for binding of leucine were conserved in hGDH2. The mutational analyses of hGDH2 revealed that hGDH2 was also allosterically activated by leucine with a similar manner with GDH from T. thermophilus.
We also performed comprehensive analysis of gene regulation by means of DNA microarray tecnique and suggested that leucine was a signal of global regulation in T. thermophilus.
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Report
(3 results)
Research Products
(19 results)
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[Book] 化学2012
Author(s)
富田武郎、西山真
Total Pages
2
Publisher
化学同人
Related Report
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