2004 Fiscal Year Final Research Report Summary
Mechanism of flagellin perception in rice
| Project/Area Number |
15380084
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Bioproduction chemistry/Bioorganic chemistry
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
CHE Fang-sik Nara Institute of Science and Technology, Graduate School of Biological Sciences, Assistant Professor, バイオサイエンス研究科, 助手 (00263442)
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| Co-Investigator(Kenkyū-buntansha) |
IWANO Megumi Nara Institute of Science and Technology, Graduate School of Biological Sciences, Assistant Professor, バイオサイエンス研究科, 助手 (50160130)
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| Project Period (FY) |
2003 – 2004
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| Keywords | Plant immunity / Flagellin / Protein-protein interaction / Elicitor / Sugar chain / Rice / Disease resistance / Signal transduction |
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| Research Abstract |
The host range of Asidovorax avenae is wide among monocotyledonous but individual strains can infect only one or a few host species. Several defense responses in cultured rice cells were only induced by a rice incompatible strain. Recently we also reported that the flagellin from incompatible A.avenae was involved in the induction of these defense responses. To clarify the mechanism of flagellin perception in rice, we tried to define the region(s) of flagellin protein required for activation of defense response using the recombinant deleted proteins produced in an Escherichia coli expression system. We found that flagellin fragment containing the C-terminal region induced generation of reactive oxygen species and expression of defense-related genes in cultured rice cells, whereas the flagellin fragments containing middle or N-terminal region did not cause any defense responses. The N-terminal fragment comprises core of conserved 22 amino acids (flg22) which induce defense responses in
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tomato and Arabidopsis thaliana. In fact, the N-terminal fragment and flg22-avenae (comprising flg22 position of N1141 flagellin) induced generation of reactive oxygen species in cultured A.thaliana cells. These results suggest that the flagellin perception system in rice is different from that in A.thaliana. We next tried to identify the flagellin perception molecule in rice using yeast-two-hybrid system. Two-hybrid screening using rice cDNA library as play and C-terminal domain as bait showed that FIP50 (flagellin interacting protein) specifically interactes with C-terminal domain of flagellin. FIP50 was functional unknown protein and located in cytoplasm. Immune-precipitation assay revealed that recombinant FIP50 protein specifically binds with flagellin C-terminal protein in vitro. These results together with down regulation of FIP50 expression level by flagellin treatment suggest that FIP50 is involved in flagellin perception and transduction of flagellin perception signaling in rice. Less
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