Identification of valuable genes from a hyperthermophile by focusing attention on its transcriptional regulation network
| Project/Area Number |
22550151
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Kyoto University |
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Principal Investigator |
KANAI Tamotsu 京都大学, 大学院・工学研究科, 講師 (10346083)
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| Co-Investigator(Renkei-kenkyūsha) |
ATOMI Haruyuki 京都大学, 大学院・工学研究科, 教授 (90243047)
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| Project Period (FY) |
2010 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2011: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2010: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | 超好熱菌 / アーキア / 有用遺伝子 / 転写制御因子 / EMSA / マイクロアレイ解析 / 遺伝子 / 遺伝子制御 / 始原菌 |
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| Research Abstract |
Proteins from thermophiles are expected as a source of excellent biomaterials that can function under high temperature conditions, where chemical reactions are accelerated. This study deals with functional analysis on hypothetical genes of the hyperthermophilic archaeon, Thermococcus kodakarensis, with focusing attention onits transcriptional regulation network. As a result, a new sugar-degrading enzyme was identified that can hydrolyze maltooligosaccharides.
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Report
(4 results)
Research Products
(28 results)
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[Journal Article] Structural basis for branching-enzyme activity of glycoside hydrolase family 57: structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD12011
Author(s)
Santos, C.R., C.C. Tonoli, D.M. Trindade, C. Betzel, H. Takata, T. Kuriki, T. Kanai, T. Imanaka, R.K. Arni, and M.T. Murakami
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Journal Title
Proteins
Volume: vol.79
Issue: 2
Pages: 547-557
DOI
Related Report
Peer Reviewed
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[Journal Article] Structural basis for branching-enzyme activity of glycoside hydrolase family 57 : structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus kodakaraensis KOD12011
Author(s)
Santos, C.R., Tonoli, C.C.C., Trindade, D.M., Betzel, C., Takata, H., Kuriki, T., Kanai, T., Imanaka, T., Arni, R.K., Murakami, M.T.
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Journal Title
PROTEINS : Structure, Function, and Bioinformatics
Volume: 79
Pages: 547-557
Related Report
Peer Reviewed
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