Faculty Profiles - TOYODA Kazuhiro

MISC - TOYODA Kazuhiro

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Analysis of Pea Apoplastic Cu/Zn-SOD Responsive to Pathogenic Signal Molecules(Abstracts of the Papers Presented at the 2003 Annual Meeting in Tokyo)

Kasai T., Ono K., Toyoda K., Inagaki Y., Yamamoto M., Ichinose Y., Shiraishi T.

Annals of the Phytopathological Society of Japan 69 ( 3 ) 250 - 250 2003.8

Characterization of Plasma Membrane Proteins Affinity-purified with Concanavalin A (Con A), a Potent Elicitor of Phytoalexin Accumulation(Abstracts of the Papers Presented at the 2003 Annual Meeting in Tokyo)

Okazaki A., Toyoda K., Sugimoto M., Inagaki Y., Yamamoto M., Ichinose Y., Shiraichi T.

Annals of the Phytopathological Society of Japan 69 ( 3 ) 249 - 250 2003.8

Construction of subracted cDNA Library of Strawberry Treated by AF-toxins from Alternaria alternata Strwberry Pathotype(Abstracts of the Papers Presented at the 2003 Annual Meeting in Tokyo)

Kitani K., Toyoda K., Shiraishi T., Yamamoto M.

Annals of the Phytopathological Society of Japan 69 ( 3 ) 252 - 253 2003.8

Flagellin-induced HR Cell Death Is Independent of Type III Secretion System in Pseudomonas syringae pv. tabaci(Abstracts of the Papers Presented at the 2003 Annual Meeting in Tokyo)

Marutani M., Taguchi F., Toyoda K., Inagaki Y., Shiraishi T., Ichinose Y.

Annals of the Phytopathological Society of Japan 69 ( 3 ) 300 - 301 2003.8

Medicago truncatula-Mycosphaerella pinodes Interaction, a New Model for the Molecular and Genetic Dissection of Plant-microbe Interaction

Toyoda K., Ikeda S., Morikawa J., Inagaki Y., Ichinose Y., Yamamoto M., Shiraishi T.

Annals of the Phytopathological Society of Japan 69 ( 1 ) 56 - 56 2003.2

Endogenous Suppressor in Arabidopsis thaliana

Rao U.S., Matsushita H., Toyoda K., Ichinose Y., Inagaki Y., Yamamoto M., Tsuji G., Kubo Y., Shiraishi T.

Annals of the Phytopathological Society of Japan 69 ( 1 ) 56 - 56 2003.2

Extracellular PO_4^- induces the expression of peroxidases in Pisum sativum

Kawahara T., Nanba H., Toyoda K., Inagaki Y., Ichinose Y., Yamamoto M., Shiraishi T.

Annals of the Phytopathological Society of Japan 69 ( 1 ) 56 - 57 2003.2

Characterization of elicitor-responsive receptor-like protein kinase in tobacco

Sasabe M., Toyoda K., Inagaki Y., Shiraishi T., Ichinose Y.

Annals of the Phytopathological Society of Japan 69 ( 1 ) 56 - 56 2003.2

Analysis of Suppressor-responsive Genes : (5) Expression of OPR Gene Family

Matsui H., Nakamura G., Ishiga Y., Toyoda K., Inagaki Y., Shiraishi T., Ichinose Y.

Annals of the Phytopathological Society of Japan 69 ( 1 ) 57 - 57 2003.2

Possible Involvement of AAAG Motif and PsDof1 in Elicitor-Induced Gene Expression in Pea

Seki Hikaru, Marutani Mizuri, Inagaki Yoshishige, Toyoda Kazuhiro, Shiraishi Tomonori, Ichinose Yuki

92 ( 1 ) 21 - 26 2003.2

Need for flagella for complete virulence of Pseudomonas syringae pv. tabaci : genetic analysis with flagella-defective mutants ΔfliC and ΔfliD in host tobacco plants

ICHINOSE Yuki, SHIMIZU Rena, IKEDA Yoko, TAGUCHI Fumiko, MARUTANI Mizuri, MUKAIHARA Takafumi, INAGAKI Yoshishige, TOYODA Kazuhiro, SHIRAISHI Tomonori

J. Gen. Plant Pathol. 69 ( 4 ) 244 - 249 2003

Expression of allene oxide synthase and allene oxide cyclase in the interactions between pea and fungal pathogens

ISHIGA Yasuhiro, INAGAKI Yoshishige, TOYODA Kazuhiro, SHIRAISHI Tomonori, ICHINOSE Yuki

J Gen Plant Pathol 69 ( 6 ) 351 - 357 2003

Phylogenetic Classification of Dof- type Transcription Factors in Pea (Pisum sativum)

NAKAMURA Naoki, MARUTANI Mizuri, SANEMATSU Shiroh, TOYODA Kazuhiro, INAGAKI Yoshi-shige, SHIRAISHI Tomonori, ICHINOSE Yuki

Plant tissue culture letters 20 ( 3 ) 247 - 252 2003

Language：English Publisher：Japanese Society for Plant Cell and Molecular Biology

The Dof protein family is a group of plant transcription factors carrying highly conserved 52 residues referred to as the Dof domain, and belongs to the C4 zinc-finger transcription factors. We isolated various PsDof genes by PCR using the Dof-domain nucleotide sequence of the PsDof1 gene from a cDNA library of elicitor-treated pea epicotyls, and these isolated PsDof genes were then classified phylogenetically. Since the obtained genes (PsDof1 to PsDof7) were scattered over various positions of the phylogenetic tree, they were expected to perform various functions as Dof-type transcription factors. From their positions in the tree, it is expected that the PsDof2 and PsDof5 genes are defense related, as is the PsDof1 gene.

DOI： 10.5511/plantbiotechnology.20.247

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Other Link： https://jlc.jst.go.jp/DN/JALC/00231800981?from=CiNii

Flagella-mediated Interactions between Phytopathogenic Bacteria and Plants

ICHINOSE Yuki, TAGUCHI Fumiko, INAGAKI Yoshishige, TOYODA Kazuhiro, SHIRAISHI Tomonori

41 ( 8 ) 511 - 516 2003

Post-translational modification of flagellin determines the specificity of HR induction

TAGUCHI F

Plant Cell Physiol 44 ( 3 ) 342 - 349 2003

Cloning and characterization of pea apyrases: Involvent of psAPY1 in response to signal molecules from the pea pathogen, Mycosphaerella pinodes

Journal of plant pathology 69, 33-38 2003

Differential effects of flagellins from Pseudomonas syringae pv. tabaci, tomato and glycinea on plant defense response

TAGUCHI F

Plant Physiol Biochem 41 165 - 174 2003

Role of flagella and flagellin in plant - Pseudomonas syringae interactions

Y Ichinose, R Shimizu, F Taguchi, K Takeuchi, M Marutani, T Mukaihara, Y Inagaki, K Toyoda, T Shiraishi

PSEUDOMONAS SYRINGAE AND RELATED PATHOGENS: BIOLOGY AND GENETICS pp. 311-318. 311 - 318 2003

Language：English Publisher：SPRINGER

The role of flagella and monomer flagellin of Pseudomonas syringae pv. tabaci in plant-bacteria interactions was investigated by using non-polar fliC or fliD mutants. These mutants deleted the open reading frames for fliC and fliD, respectively, and both mutants lost all flagella and motility. The DeltafliC mutant did not produce flagellin, whereas DeltafliD mutant, that lost HAP2 protein, secreted a large amount of monomer flagellin in the culture medium. Inoculation of tomato leaves with wild type and DeltafliD mutant of P. s. pv. tabaci induced HR, whereas the DeltafliC mutant caused symptom-like change and propagated as P. s. pv. tomato. In tomato suspension cultured cells, wild type P. s. pv. tabaci induced visible HR-like changes. The DeltafliC mutant did not induce the HR, but the response was activated by the DeltafliD mutant. The expression of typical defence genes such as PAL and hsr203J was rapidly and strongly induced by inoculation with the DeltafliD mutant compared to inoculation with wild type P. s. pv. tabaci. On the other hand, both fliC and fliD mutants were reduced in virulence when inoculated into host tobacco leaves. Furthermore, complementation of fliC gene in DeltafliC mutant restored motility and HR-inducing ability in tomato, and virulence in tobacco. These results suggest that the monomer flagellin of P. s. pv. tabaci is an essential factor in the elicitation of HR in non host tomato cells, and flagella are required for complete virulence in host tobacco cells.

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Resistance and susceptibility of plants to fungal pathogens

K Toyoda, NC Collins, A Takahashi, K Shirasu

TRANSGENIC RESEARCH 11 ( 6 ) 567 - 582 2002.12

Language：English Publishing type：Book review, literature introduction, etc. Publisher：KLUWER ACADEMIC PUBL

Plants are under continuous threat of infection by pathogens endowed with diverse strategies to colonize their host. Comprehensive biochemical and genetic approaches are now starting to reveal the complex signaling pathways that mediate plant disease resistance. Initiation of defense signaling often involves specific recognition of invading pathogens by the products of specialized host resistance (R) genes. Potential resistance signaling components have been identified by mutational analyses to be required for specific resistance in the model Arabidopsis and some crop species. Strikingly, many of the components share similarity to that of innate immune systems in animals. Evidence is also accumulating that plant pathogens have a number of ways to evade host defenses during the early stages of infection, similar to animal pathogens. These strategies are becoming much better understood in a number of plant- pathogen interactions. In this review, we focus on the current knowledge of host factors that control plant resistance and susceptibility to fungal pathogens. The knowledge accumulated in these studies will serve a fundamental basis for combating diseases in strategic molecular agriculture.

DOI： 10.1023/A:1021182111770

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Expression of the 12-oxophytodienoic acid 10,11-reductase gene in the compatible interaction between pea and fungal pathogen

Y Ishiga, A Funato, T Tachiki, K Toyoda, T Shiraishi, T Yamada, Y Ichinose

PLANT AND CELL PHYSIOLOGY 43 ( 10 ) 1210 - 1220 2002.10

Language：English Publisher：OXFORD UNIV PRESS

Suppressors produced by Mycosphaerella pinodes are glycopeptides to block pea defense responses induced by elicitors. A clone, S64, was isolated as cDNA for suppressor-inducible gene from pea epicotyls. The treatment of pea epicotyls with suppressor alone induced an increase of S64 mRNA within 1 h, and it reached a maximum level at 3 h after treatment. The induction was not affected by application of the elicitor, indicating that the suppressor has a dominant action to regulate S64 gene expression. S64 was also induced by inoculation with a virulent pathogen, M. pinodes, but not by inoculation with a non-pathogen, Ascochyta rabiei, nor by treatment with fungal elicitor. The deduced structure of S64 showed high homology to 12-oxophytodienoic acid reductase (OPR) in Arabidopsis thaliana. A recombinant protein derived from S64 had OPR activity, suggesting compatibility-specific activation of the octadecanoid pathway in plants. Treatment with jasmonic acid (JA) or methyl jasmonic acid, end products of the octadecanoid pathway, inhibited the elicitor-induced accumulation of PAL mRNA in pea. These results indicate that the suppressor-induced S64 gene expression leads to the production of JA or related compounds, which might contribute to the establishment of compatibility by inhibiting the phenylpropanoid biosynthetic pathway.

DOI： 10.1093/pcp/pcf144

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