Functional analysis of plant pathogen effector proteins in yeast and its application
Project/Area Number |
25450104
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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 microbiology
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Research Institution | Kagawa University |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
TANAKA NAOTAKA 香川大学, 農学部, 准教授 (60324109)
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Project Period (FY) |
2013-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | 病原菌エフェクター / グルタチオン / 酵母 / チオレドキシン / 青枯病菌 / Saccharomyces cerevisiae / レドックス制御 / 病害抵抗性 / エフェクター / レドックス / 病原性 |
Outline of Final Research Achievements |
The plant pathogenic bacterium Ralstonia solanacearum injects more than 70 effector proteins into the host plant cells via needle-like structure of a type Ⅲ secretion system. The effector proteins manipulate host cellular functions with diverse molecular activities. The understanding of the molecular function of effectors is essential to uncover the molecular mechanism for pathogenesis of R. solanacearum-infection. Here, we show that a ChaC-like domain containing effector RipAY from R. solanacearum exhibits γ-glutamyl cyclotransferase (GGCT) activity to degrade the major intracellular redox buffer, glutathione, which is known to be crucial for a proper activation of host immune defense in plants. Intriguingly, RipAY protein exhibits a robust GGCT activity by the interaction with eukaryotic thioredoxins, which are also important for intracellular redox homeostasis during bacterial infection in plants.
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Report
(4 results)
Research Products
(25 results)
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[Journal Article] RipAY, a plant pathogen effector protein, exhibits robust γ-glutamyl cyclotransferase activity when stimulated by eukaryotic thioredoxins.2016
Author(s)
Fujiwara S., Kawazoe T., Ohnishi K., Kitagawa T., Popa C., Valls M., Genin S., Nakamura K., Kuramitsu Y., Tanaka N. and Tabuchi M.
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Journal Title
Journal of Biological Chemistory
Volume: 291
Issue: 13
Pages: 6813-30
DOI
Related Report
Int'l Joint Research / Acknowledgement Compliant
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[Journal Article] VPS35 dysfunction impairs lysosomal degradation of α-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease.2014
Author(s)
Miura E, Hasegawa T, Konno M, Suzuki M, Sugeno N, Fujikake N, Geisler S, Tabuchi M, Oshima R, Kikuchi A, Baba T, Wada K, Nagai Y, Takeda A, Aoki M.
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Journal Title
Neurobiol Dis.
Volume: 71
Pages: 1-13
Related Report
Peer Reviewed
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