Faculty Profiles - ICHINOSE Yuki

MISC - ICHINOSE Yuki

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(322)Hypersensitive Response-Inducing Factors Produced by Pseudomonas syringae (6) Putative Genomic Island Involved in Flagellin Glycosylation of P. syringae

Takeuchi K, Kawasaki T, Taguchi F, Shimizu R, Ikeda Y, Inagaki Y, Shiraishi T, Ichinose Y

Annals of the Phytopathological Society of Japan 68 ( 2 ) 243 - 243 2002.8

Hypersensitive Response-Inducing Factors Produced by Pseudomonas syringae (4) Functional Analysis of Flagellin Using Flagella-Deficient Mutants(Abstracts Presented at the Meeting of the Kansai Division)

Shimizu R, Taguchi F, Ikeda Y, Toyoda K, Shiraishi T, Inagaki Y, Ichinose Y

Annals of the Phytopathological Society of Japan 68 ( 1 ) 100 - 100 2002.4

Pseudomonas syringae pv. tabaciの単量体Flagellinは,非宿主植物トマト細胞にHR誘導因子として働く

清水鈴菜, 田口富美子, 池田陽子, 豊田和弘, 白石友紀, 稲垣善茂, 一瀬勇規

日本植物生理学会年会要旨集 42nd 238 2002.3

HR誘導性細菌エリシターflagellinのHR誘導及び病原性における翻訳後修飾の重要性

田口富美子, 池田陽子, 清水鈴菜, 竹内香純, 稲垣善茂, 白石友紀, 一瀬勇規

日本植物生理学会年会要旨集 42nd 238 2002.3

cDNA cloning and characterization of tobacco ABC transporter: NtPDR1 is a novel elicitor-responsive gene.

FEBS Letters 518, 164-168 2002

Molecular cloning of cDNA for a novel pea Dof protein, PsDof1, and its DNA binding activity to the promoter of PsDof1 gene.

SEKI Hikaru, NAKAMURA Naoki, MARUTANI Mizuri, OKABE Takeharu, SANEMATSU Shiroh, INAGAKI Yoshishige, TOYODA Kazuhiro, SHIRAISHI Tomonori, YAMADA Tetsuji, ICHINOSE Yuki

Plant Biotechnol. 19 ( 4 ) 251 - 260 2002

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

A cDNA clone, designated PsDof1, encoding a novel member of the Dof DNA-binding protein family was isolated from pea. Random-binding-site selection and gel retardation experiments showed that the GST-PsDof1 recombinant protein bound to specific DNA sequences with an AAAG core. A metal-chelating agent, 1, 10-phenanthroline, abolished binding of GST-PsDof1 to DNA, but the addition of Zn²⁺ restored it, indicating that zinc ions are required for its DNA-binding activity. Interestingly, there are possible sites for binding PsDof1 in its promoter sequence. Indeed, GST-PsDof1 binds to the AAAG-containing promoter sequence of the PsDof1 gene with higher affinity. These results suggest that PsDof1 is a novel transcription factor that is involved in its own transcriptional regulation.

DOI： 10.5511/plantbiotechnology.19.251

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Other Link： https://jlc.jst.go.jp/DN/JALC/00161151771?from=CiNii

Molecular Cloning of cDNA for a Novel Pea Dof Protein, PsDof1, and Its DNA-Binding Activity to the Promoter of PsDof1 Gene

SEKI Hikaru, NAKAMURA Naoki, MARUTANI Mizuri, OKABE Takeharu, SANEMATSU Shiroh, INAGAKI Yoshishige, TOYODA Kazuhiro, SHIRAISHI Tomonori, YAMADA Tetsuji, ICHINOSE Yuki

Plant tissue culture letters 19 ( 4 ) 251 - 260 2002

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

DOI： 10.5511/plantbiotechnology.19.251

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Other Link： https://jlc.jst.go.jp/DN/JALC/00161151771?from=CiNii

Flagellin, a constituent of a flagella filament in Pseudomonas syringae pv. tabaci, is an intense HR elicitor as a monomer molecule on nonhost tomato cells

R Shimizu, F Taguchi, Y Ikeda, K Toyoda, T Shiraishi, Y Inagaki, Y Ichinose

PLANT AND CELL PHYSIOLOGY 43 S201 - S201 2002

Cell wall-plasma membrane continuum is involved in transduction of pathogen signals

K Toyoda, AM Kiba, T Kawahara, M Sugimoto, RS Uppalapati, Y Inagaki, Y Ichinose, M Yamamoto, T Shiraishi

PLANT AND CELL PHYSIOLOGY 43 S10 - S10 2002

The importance of post-translational modification of bacterial HR-elicitor, flagellin on HR-inducing ability and pathogenicity

F Taguchi, Y Ikeda, R Shimizu, K Takeuchi, Y Inagaki, T Shiraishi, Y Ichinose

PLANT AND CELL PHYSIOLOGY 43 S201 - S201 2002

Biochemical and molecular biological studies on infection (Ascochyta rabiei)-induced thaumatin-like proteins from chickpea plants (Cicer arietinum L.)

T Hanselle, Y Ichinose, W Barz

ZEITSCHRIFT FUR NATURFORSCHUNG C-A JOURNAL OF BIOSCIENCES 56 ( 11-12 ) 1095 - 1107 2001.11

Language：English Publisher：VERLAG Z NATURFORSCH

A pathogenesis-related protein induced by infection with Ascochyta rabiei was purified from intercellular washing fluid of chickpea (Cicer arietinum L.) leaves. Amino-terminal sequencing identified the protein, named PR-5a, as a thaumatin-like protein. The isoelectric point was determined with 6.5 and the molecular mass is 16 kDa. Therefore., chickpea PR-5a is the first dicot member of a TLP subgroup containing small TLPs with a molecular weight between 15 and 18 kDa. PR-5a shows no antifungal activity towards A. rabiei. Screening of a chickpea cDNA library led to the isolation of a cDNA clone (p5a-241) for this protein. A second cDNA clone (ELR112) encoding a TLP was isolated using differential hybridisation of cDNA libraries obtained from elicited and water treated cell suspension cultures of chickpea. The deduced protein (PR-5b) has a molecular mass of 22 kDa. PR-5b is postulated to be located in the vacuole due to the presence of a respective N-terminal signal peptide and a carboxy-terminal extension. Southern blot analyses showed that ELR112 and p5a-241 represent single copy genes. During fungal infection of chickpea plants expression of both genes proceeds much faster in an A. rabiei resistant cultivar than in a susceptible one.

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Generation of hydrogen peroxide is not required for harpin-induced apoptotic cell death in tobacco BY-2 cell suspension culture

Y Ichinose, S Andi, R Doi, R Tanaka, F Taguchi, M Sasabe, K Toyoda, T Shiraishi, T Yamada

PLANT PHYSIOLOGY AND BIOCHEMISTRY 39 ( 9 ) 771 - 776 2001.9

Authorship：Lead author Language：English Publisher：GAUTHIER-VILLARS/EDITIONS ELSEVIER

To characterize molecular and biochemical mechanisms of hypersensitive reaction (HR) in plants, a tobacco suspension culture of BY-2 was treated with the proteinaceous HR elicitor harpin from several pathovars of Pseudomonas syringae. Tobacco BY-2 cells are sensitive to harpins derived from non-pathogenic pathovars of P. syringae, such as pvs. pisi, tomato and glycinea. These three harpins induce apoptotic cell death accompanied by DNA fragmentation in BY-2. Because the cell death was also accompanied by rapid generation of hydrogen peroxide (H2O2), one of the active oxygen species, we investigated the role of H2O2 in harpin-induced cell death. Although treatment with diphenylene iodium chloride (DPI) reduced, and catalase completely abolished, the harpin-induced generation of H2O2, the frequency of cell death was not affected at all. Treatment with superoxide dismutase (SOD) enhanced the generation of H2O2, but the cell death was unaffected. These results indicate that harpin-induced apoptotic cell death does not require oxidative burst. (C) 2001 Editions scientifiques et medicales Elsevier SAS

DOI： 10.1016/S0981-9428(01)01300-6

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Contrary operations of Box-I element of pea phenylalanine ammonia-lyase gene 1 promoter for organ-specific expression

Y Imura, H Seki, K Toyoda, Y Ichinose, T Shiraishi, T Yamada

PLANT PHYSIOLOGY AND BIOCHEMISTRY 39 ( 5 ) 355 - 362 2001.5

Language：English Publisher：GAUTHIER-VILLARS/EDITIONS ELSEVIER

Expression of genes (PSPAL) encoding phenylalanine ammonia-lyase from pea (Pisum sativum L.) is regulated in response to various environmental stimuli and during plant development. We examined the cis-regulatory elements in PSPAL1 promoter for organ-specific expression by determining the sequences specifically associated with nuclear proteins on its promoter in each pea organ. In vivo dimethyl sulfate (DMS) footprinting analysis showed putative protein bindings on AC-rich sequences including Box-I in particular in roots and stems in which PSPAL mRNA were highly accumulated. The potential role of the AC-rich element was investigated by fusing PSPAL1 promoter with Box-I deleted to the reporter gene P-glucuronidase (GUS) and transforming the construct into tobacco plants (Nicotiana tabacum). GUS activity controlled under this Box-I deletion promoter was significantly reduced in roots and leaves, whereas drastically increased in stems as compared with the activity of wild-type PSPALI promoter. Histochemical GUS staining indicated the activity was elevated in vascular tissues of stem by deleting Box-I. These results suggest that Box-I in PSPALI contributes to a positive regulation in root and leaf, but might also function as a negative regulator in stem, especially in xylem tissue. (C) 2001 Editions scientifiques et medicales Elsevier SAS.

DOI： 10.1016/S0981-9428(01)01248-7

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Molecular cloning and functional analysis of pea cDNA E86 encoding homologous protein to hypersensitivity-related hsr203J

Y Ichinose, Y Hisayasu, S Sanematsu, Y Ishiga, H Seki, K Toyoda, T Shiraishi, T Yamada

PLANT SCIENCE 160 ( 5 ) 997 - 1006 2001.4

Language：English Publisher：ELSEVIER SCI IRELAND LTD

Clone E86 was isolated as cDNA for elicitor-inducible gene From pea epicotyls by differential screening. The deduced amino acid sequence of E86 showed high homology to hypersensitivity-related protein hsr203J in tobacco and also showed significant homologies to the Ser-active hydrolases, such as mammalian hormone-sensitive lipases, bacterial lipases and esterases. E86 polypeptide possesses consensus amino acid sequence motifs (His-Gly) and (Gly-X-Ser-X-Gly) conserved in lipases and esterases and showed esterase degradation of p-nitrophenyl butyrate. Northern blot analysis revealed that the E86-transcript is abundant in roots and stems and was induced by fungal elicitor in pea epicotyls. However, elicitor-induced accumulation of E86 mRNA was significantly inhibited by the fungal suppressor. Furthermore the expression of the genes encoding E86 and phenylalanine ammonia-lyase was induced within 1 h after the inoculation of a nonpathogen. but it was delayed for 5 h by the inoculation of a compatible pathogen. These results suggest that the elicitor-induced Ser-active hydrolase derived from E86 gene might be related to the plant defense responses. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

DOI： 10.1016/S0168-9452(01)00343-0

Bacteriophage P4282, a parasite of Ralstonia solanacearum, encodes a bacteriolytic protein important for lytic infection of its host

H Ozawa, H Tanaka, Y Ichinose, T Shiraishi, T Yamada

MOLECULAR GENETICS AND GENOMICS 265 ( 1 ) 95 - 101 2001.3

Language：English Publisher：SPRINGER-VERLAG

To enhance bacterial wilt resistance in tobacco expressing a foreign protein, we isolated the bacteriolytic gene from a bacteriophage that infects Ralstonia solanacearum The bacteriolytic protein of phage P4282 isolated in Tochigi Prefecture was purified from a lysate of R. solanacearum M4S cells infected with the phage, and its bacteriolytic activity was assayed by following the decrease in the turbidity of suspensions of R. solanacearum M4S cells. The molecular weight of the bacteriolytic protein was approximately 71 kDa, and the sequence of the N-terminal 13 amino acids was determined. We used oligonucleotide probes based on this amino acid sequence to isolate the bacteriolytic gene from phage P4282 DNA. This gene of 2061 bp encodes a product of 687 amino acids, whose calaculated molecular weight was 70.12 kDa. The bacteriolytic gene was placed under the control of an inducible promoter, and the plasmid was transformed into Escherichia coli NM522. The soluble proteins extracted from E. coli NM522 cells harboring the plasmid with the bacteriolytic gene showed obvious bacteriolytic activities against several strains of R. solanacearum isolated in various districts in Japan. DNA fragments from five phages, isolated in Niigata. Aomori, Okinawa, Fukushima and Yamaguchi Prefectures, hybridized to the bacteriolytic gene of phage P4282. These observations indicate that the bacteriolytic protein shows nonspecific activity against R. solanacearum strains, and a sequence similar to that of the bacteriolytic gene is conserved in the DNA of other bacteriophages. These results indicate that the generation of transgenic (tobacco) plants expressing the bacteriolytic gene of phage P4282 might result in enhanced resistance to bacterial wilt in tobacco.

DOI： 10.1007/s004380000389

Bacteriophage P4282, a parasite of Ralstonia solanacearum, encodes a bacteriolytic protein important for lytic infection of its host

H Ozawa, H Tanaka, Y Ichinose, T Shiraishi, T Yamada

MOLECULAR GENETICS AND GENOMICS 265 ( 1 ) 95 - 101 2001.3

Language：English Publisher：SPRINGER-VERLAG

DOI： 10.1007/s004380000389

Harpin_Psta from ┣DB Pseudomonas syringae (/)-┫DB pv.┣DB tabaci (/)-┫DB is defective and deficient in its gene expression and HR-inducing activity.

J. Gen. Plant Pathol. 67 ( 2 ) 116 - 123 2001

Effect of harpin from four pathovars of ┣DB Pseudomonas syringae (/)-┫DB on pea defense responses.

J. Gen. Plant Pathol. 67 ( 2 ) 148 - 151 2001

Effect of Harpin from Four Pathovars of Pseudomonas syringae on Pea Defense Responses (Short Communication) :

TANAKA Rui, TAGUCHI Fumiko, ICHINOSE Yuki, TOYODA Kazuhiro, SHIRAISHI Tomonori, YAMADA Tetsuji

Journal of general plant pathology : JGPP 67 ( 2 ) 148 - 151 2001

Language：English Publisher：Phytopathological Society of Japan

To investigate the role of the proteinaceous elicitor, harpin, on host and nonhost plants, we isolated the harpin-coding gene, hrpZ, from Pseudomonas syringae pvs. pisi, glycinea, tabaci and tomato. Effects of the recombinant harpin proteins on pea plants were analyzed and compared with the effects of the corresponding bacterial treatment. After inoculation of pea with pea pathogen P. syringae pv. pisi, the bacterial population increased and the accumulation of PAL-mRNA and pisatin was inhibited. The nonpathogenic pathovars, glycinea, tabaci and tomato induced both defense responses in pea. However, none of the harpins induced the hypersensitive reaction or accumulation of PAL-mRNA and pisatin in pea. Harpins from P. syringae pvs. glycinea, tomato and pisi did induce these defense responses in tobacco, however, suggesting that externally applied harpins either are not recognized or are nonfunctional in pea plants. (Received July 27, 2000 ; Accepted February 21, 2001)

DOI： 10.1007/PL00013001

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Other Link： http://id.nii.ac.jp/1141/00138226/

初期・表層シグナル伝達系と防御システム

化学と生物 39 ( 10 ) 531 - 537 2001

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