| Project/Area Number |
26870113
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Applied biochemistry
Applied microbiology
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| Research Institution | The University of Tokyo |
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Principal Investigator |
Yoshida Ayako 東京大学, 生物生産工学研究センター, 特任助教 (90633686)
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| Co-Investigator(Renkei-kenkyūsha) |
KOSONO Saori 東京大学, 生物生産工学研究センター, 特任准教授 (90321760)
NISHIYAMA Makoto 東京大学, 生物生産工学研究センター, 教授 (00208240)
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2014: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | タンパク質アシル化修飾 / タンパク質アセチル化酵素 / アミノ酸代謝 / CoA体代謝 / 代謝調節 / タンパク質間相互作用 / タンパク質相互作用 / タンパク質翻訳後修飾 / 短鎖アシル化 / Thermus thermophilus |
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| Outline of Final Research Achievements |
The proteomic analysis revealed that a lot of proteins were acetylated and succinylated in Thermus thermophilus HB27. 2-isopropylmalate synthase (IPMS), which catalyzes the first step of leucine biosynthesis, is both acetylated and succinylated. The acylation-mimic mutant showed the lower activity and changed the substrate specificity. We suppose that the acylation on IPMS may regulate the flux of branched-chain amino acids.
The analysis of protein lysine acetyltransferase (KAT) from T. thermophilus identified the CoA transferase as an acetylation substrate of KAT. Since this CoA transferase uses Acetyl-CoA, which is a substrate of KAT, suggesting that the acetylation of CoA transferase regulates CoA metabolism depending on the concentration of Acetyl-CoA. Moreover, we found the protein interacting with this CoA transferase, suggesting that the activity of CoA transferase is regulated in a complex manner including protein acylation and regulatory protein binding.
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