Identification of the physiological role of inositol kinase and inositol monophosphate in Archaea
| Project/Area Number |
26850049
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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 microbiology
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| Research Institution | Kyoto University |
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Principal Investigator |
Sato Takaaki 京都大学, 工学研究科, 助教 (60571411)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
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| Keywords | Inositol / Kinase / Archaea / Hyperthermophile / イノシトール / キナーゼ / アーキア / 高温ストレス適応 / 適合溶質 / 高温ストレス応答 / inositol / イノシトールキナーゼ / 代謝 / 遺伝子破壊 / 反応産物同定 / 発現活性化条件同定 / 微生物 |
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| Outline of Final Research Achievements |
The purpose of this study is to identify the physiological role of myo-inositol kinase and its product, myo-inositol phosphate, in Archaea. The reaction product of the archaeal inositol kinase was identified to be inositol 3-phosphate whose hydroxyl group at C3 position is phosphorylated among six hydroxyl groups. Inositol 3-phosphate is generally synthesized from glucose 6-phosphate, which can be the substrate to synthesize a compatible solute. In addition, in vivo analyses of its gene transcription levels and gene disruption strain suggested that this enzyme is involved in the response to environmental stress. These results obtained in this study suggested that the myo-inositol kinase phosphorylates an inositol, generated with some kind of metabolism, to synthesize compatible solutes.
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| Academic Significance and Societal Importance of the Research Achievements |
原核生物においてはイノシトールという糖アルコールは環境変化に対応するための適合溶質の原料となったり、真核生物においてはシグナル伝達物質となったりする。原核生物であるアーキアにおいてイノシトールをリン酸化する酵素が見つかったが、一般的には適合溶質の生合成にリン酸化のステップはないことから、その生理的役割は不明であった。本研究では、酵素の解析や遺伝子破壊株を使った実験により、イノシトールをリン酸化する酵素の役割がやはり環境ストレスへの適応であることを示唆する知見を得た。適合溶質の生合成もしくは再生に関して今までは知られていなかった経路が存在することが示唆され、新たな研究への展開が期待される。
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Report
(4 results)
Research Products
(8 results)
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[Presentation] Functional characterization of three ribokinase family proteins in the hyperthermophilic archaeon Thermococcus kodakarensis2016
Author(s)
Takaaki Sato, Riku Aono, Masahiro Fujihashi, Yukika Miyamoto, Keiko Kuwata, Eriko Kusaka, Haruo Fujita, Kunio Miki, Tadayuki Imanaka, and Haruyuki Atomi
Organizer
The 14th China-Japan-Korea Joint Symposium on Enzyme Engineering
Place of Presentation
Guangxi Wharton International Hotel, Nanning, China
Related Report
Int'l Joint Research
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[Presentation] Novel metabolic pathways in Archaea2014
Author(s)
Takaaki Sato, Riku Aono, Sanae Hodo, Yuta Yoshii, Tadayuki Imanaka, and Haruyuki Atomi
Organizer
2014 Korean Society for Microbiology and Biotechnology International Symposium & Annual Meeting
Place of Presentation
Busan, Korea
Year and Date
2014-06-26
Related Report
Invited
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[Presentation] Functional characterization of three ribokinase family proteins in the hyperthermophilic archaeon Thermococcus kodakarensis2014
Author(s)
Takaaki Sato, Riku Aono, Masahiro Fujihashi, Yukika Miyamoto, Keiko Kuwata, Eriko Kusaka, Haruo Fujita, Kunio Miki, Tadayuki Imanaka, and Haruyuki Atomi
Organizer
American Society for Microbiology 114th General Meeting
Place of Presentation
Boston, USA
Year and Date
2014-05-18
Related Report
