Molecular mechanism of activation of signal compounds regulating resistance against pathogen in plants
Project/Area Number |
15K07379
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Applied biochemistry
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Research Institution | Hokkaido University |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
佐分利 亘 北海道大学, 農学研究院, 助教 (00598089)
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Project Period (FY) |
2015-10-21 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
|
Keywords | β-グルコシダーゼ / ツベロン酸 / ジャスモン酸 / サリチル酸 / イネ / シロイヌナズナ |
Outline of Final Research Achievements |
In plants, physiologically active compounds are inactivated by glycosylation and activated by hydrolysis of glycosides. In this study, rice beta-glucosidase TAGG2, which has high activity towards both tuberonic acid (TA) beta-glucoside and salicylic acid beta-glucoside (SAG), was biochemically and physiologically characterized. Important amino acid residues involved in recognition of SAG were determined through site-directed mutagenesis, and localization of TAGG2 to apoplast was confirmed using transgenic rice expressing a fusion protein of GFP and TAGG2. In transgenic rice expressing TAGG2, over-accumulation of TA was observed but SA level was not changed significantly. Blast infection analysis suggested overexpression of the TAGG2 gene negatively regulated the resistance against pathogens. Homologous enzymes in Arabidopsis had high activity towards oligosaccharide substrates such as laminarioligosaccharide rather than SAG.
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Report
(4 results)
Research Products
(7 results)
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[Journal Article] Structural analysis of the α-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism.2015
Author(s)
Shen X, Saburi W, Gai Z, Kato K, Ojima-Kato T, Yu J, Komoda K, Kido Y, Matsui H, Mori H, Yao M
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Journal Title
Acta Crystallogr. D Biol. Crystallogr.
Volume: 71
Issue: 6
Pages: 1382-1391
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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[Journal Article] Identification of rice Os4BGlu13 as a β-glucosidase which hydrolyzes gibberellin A4 1-O-β-D-glucosyl ester, in addition to tuberonic acid glucoside and salicylic acid derivative glucosides.2015
Author(s)
Hua, Y., Ekkhara, W., Sansenya, S., Srisomsap, C., Roytakul, S., Saburi, W., Takeda, R., Matsuura, H., Mori, H., and Ketudat Cairns, J.R.
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Journal Title
Arch. Biochem. Biophys.
Volume: 583
Pages: 36-46
DOI
Related Report
Peer Reviewed / Int'l Joint Research
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