Faculty Profiles - ICHINOSE Yuki

MISC - ICHINOSE Yuki

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Analysis of cis-regulatory elements involved in the activation of a member of chalcone synthase gene family (PsChs1) in pea

H Seki, Y Ichinose, H Kato, T Shiraishi, T Yamada

PLANT MOLECULAR BIOLOGY 31 ( 3 ) 479 - 491 1996.6

Language：English Publisher：KLUWER ACADEMIC PUBL

Cis-regulatory elements involved in the activation of the plant defense-related gene encoding chalcone synthase 1 (PsChs1) in pea (Pisum sativum L.) were examined by transient transfection, gel mobility shift assay and in vitro DNase I-footprinting analysis. Transient transfection assay revealed that a 61 bp DNA fragment spanning from -242 to -182 of PsChs1 was required for the maximal promoter activity and possibly involved in the enhancement of elicitor-mediated activation. Nuclear isolate from elicitor-treated pea epicotyl tissues contained some factor(s) that specifically bound to this DNA fragment to form a complex with low mobility (LMC, low mobility complex) in gel mobility shift assay. DNase I-footprinting analysis of LMC revealed that among three protected regions detected in a 61 bp DNA fragment, two regions contained identical AT-rich sequence, TAAAATACT. Site directed mutation in either or both identical sequences, T<(AA)under bar>AATACT to T<(GG)under bar>AATACT, resulted in the reduction or loss in the ability to form LMC. Detailed analysis of 61 bp DNA fragment demonstrated that the region from -242 to -226 containing promoter-distal TAAAATACT motif was imperative for the maximal elicitor-mediated activation of PsChs1.

DOI： 10.1007/BF00042222

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Specific response of partially purified cell wall-bound ATPases to fungal suppressor

A Kiba, K Toyoda, Y Ichinose, T Yamada, T Shiraishi

PLANT AND CELL PHYSIOLOGY 37 ( 2 ) 207 - 214 1996.3

Language：English Publisher：JAPANESE SOC PLANT PHYSIOLOGISTS

It was found that NTPases were bound to cell walls of pea and cowpea. The suppressor in pycnospore germination fluid of a pea pathogen, Mycosphaerella pinodes, inhibited the ATPase activity in the fraction, which was solubilized from pea cell wall with 0.5% Triton X-100, in a dose-dependent manner, but rather enhanced that from cowpea cell wall even at the concentration of 1 mu g ml(-1). Inhibition by the suppressor of pea cell wall-bound ATPase was a mixed type of competitive and noncompetitive. Triton X-100 PAGE and active staining of ATPase indicated that both Triton X-100 solubilized fractions contained plural molecules that hydrolyze ATP. The M(r)s of cell wall-bound ATPases seem to be considerably different from those of plasma membranes, and the number of cell wall-bound ATPase molecules were different between pea and cowpea. The electroeluted fractions corresponding to the bands of active-stained ATPases were also able to hydrolyze NTP and PPi. The respective electroeluted ATPases also showed the species-specific response to the suppressor. These results may confirm our previous concept that putative receptors for the suppressor might tightly bind to cell wall-bound ATPase or that the ATPase might be the receptor itself.

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REGULATION OF THE GENE ENCODING PHENYLALANINE AMMONIA-LYASE OF PEA IN TRANSGENIC TOBACCO

IMURA Yoshiyuki, MORIKAWA Akiko, MICHAELZACK Dalius, ICHINOSE Yuki, SHIRAISHI Tomonori, YAMADA Tetsuji

37 54 - 54 1996.3

MOLECULAR EVOLUTION OF DEFENSE RELATED CHALCONE SYNTHASE GENES IN PEA

ITOH Masayuki, ICHINOSE Yuki, SHIRAISHI Tomonori, YAMADA Tetsuji

37 54 - 54 1996.3

Suppression of ATPase Activity in Pea Cells during Infection by a Compatible Race of Pseudomonas syringae pv. pisi

SHIMOTSUMA Natsumi, HAYASHI Masaharu, MALIK Kamal A., ICHINOSE Yuki, SHIRAISHI Tomonori, YAMADA Tetsuji

Annals of the Phytopathological Society of Japan 62 ( 5 ) 498 - 501 1996

Species-specific suppression of superoxide-anion generation of surfaces of pea leaves by the suppressor from Mycosphaerella pinodes(共著)

Annals of the Phytopathological Society of JAPAN 62 ( 5 ) 508 - 512 1996

Species-specific Suppression of Superoxide-anion Generation on Surfaces of Pea Leaves by the Suppressor from Mycosphaerella pinodes

KIBA Akinori, TOYODA Kazuhiro, ICHINOSE Yuki, YAMADA Tetsuji, SHIRAISHI Tomonori

Annals of the Phytopathological Society of Japan 62 ( 5 ) 508 - 512 1996

Analysis of cis-regulatory elements involued in the activation of a member of chalcoue synthase gene family (PsCHS1) in pea(共著)

Plant Molecular Biology 1996

Suppression of ATPase activity in pea cells during infecfion by a compatible race of Pseudomouas syriugae pv. pisi(共著)

SHIMOTSUMA Natsumi, HAYASHI Masaharu, MALIK Kamal A., ICHINOSE Yuki, SHIRAISHI Tomonori, YAMADA Tetsuji

Annals of Phytopathological Society of Japan 62 ( 5 ) 498 - 501 1996

EXPRESSION OF HETEROLOGOUS PAL GENE IN MUSKMELON (CUCUMIS-MELO L CV BIRDIE)

NM SALEH, SH TAN, Y ICHINOSE, T YAMADA

ASIA-PACIFIC JOURNAL OF MOLECULAR BIOLOGY AND BIOTECHNOLOGY 3 ( 3 ) 206 - 214 1995.9

Language：English Publisher：MALAYSIAN SOC MOLECULAR BIOLOGY BIOTECHNOLOGY

A system to develop PAL gene expression using particle gun was established in Cucumis melo L. These techniques enable us to study the regulation of pea phenylalanine ammonia-lyase (PAL) promoters in a heterologous plant system. The effect of UV irradiation on the regulation of the PAL promoters under different regime of UV irradiation were tested on the mesophyll protoplasts of melon. Maximum induction of GUS expression were observed in muskmelon leaves electroporated with two members of pea PAL promoters, PSPAL1 and PSPAL2 at 120 sec and 80 sec, respectively. Further confirmation of the GUS expression in the tissue of muskmelon were carried out using particle bombardment. Similar pattern of induction of GUS expression by UV irradiation have been observed, which suggests that common mechanism of PAL gene expression may exist in both muskmelon plant.

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EXPRESSION OF HETEROLOGOUS PAL GENE IN MUSKMELON (CUCUMIS-MELO L CV BIRDIE)

NM SALEH, SH TAN, Y ICHINOSE, T YAMADA

ASIA-PACIFIC JOURNAL OF MOLECULAR BIOLOGY AND BIOTECHNOLOGY 3 ( 3 ) 206 - 214 1995.9

Language：English Publisher：MALAYSIAN SOC MOLECULAR BIOLOGY BIOTECHNOLOGY

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PLANT-LECTINS INDUCE THE PRODUCTION OF A PHYTOALEXIN IN PISUM-SATIVUM

K TOYODA, K MIKI, Y ICHINOSE, T YAMADA, T SHIRAISHI

PLANT AND CELL PHYSIOLOGY 36 ( 5 ) 799 - 807 1995.7

Language：English Publisher：JAPANESE SOC PLANT PHYSIOLOGISTS

The effects of several plant lectins on the production of a pea phytoalexin, pisatin, were examined. Con A, PHA, PNA and PSA each induced the production of pisatin in pea epicotyl tissues, demonstrating that plant lectins can act as elicitors. The production of pisatin in response to PHA, PNA or PSA was not affected by the simultaneous presence of the respective hapten sugars, whereas haptens specific for Con A, such as alpha-D-mannose and methyl-alpha-D-mannoside, abolished the induction of pisatin by Con A. These results indicate that the elicitor effect of Con A is attributable to its ability to bind to specific carbohydrates in pea cells. Induction of the production of pisatin by Con A was markedly inhibited by the suppressor derived from a pea pathogen. Mycosphaerella pinodes, and by several inhibitors related to signal-transduction pathways. It is suggested, therefore, that the Con A-induced production of pisatin in pea tissues might be associated with activation of a signal-transduction pathway. An additive effect on the accumulation of pisatin was observed when Con A was present with a polysaccharide elicitor from M. pinodes, suggesting that exogenous Con A does not compete with the recognition site(s) for the fungal elicitor in pea cells. The present data also indicate that Con A may be useful for characterization of the signal-transduction system that leads to the synthesis of phytoalexin in pea epicotyl tissues.

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SPECIFIC-INHIBITION OF CELL WALL-BOUND ATPASES BY FUNGAL SUPPRESSOR FROM MYCOSPHAERELLA-PINODES

A KIBA, K TOYODA, Y ICHINOSE, T YAMADA, T SHIRAISHI

PLANT AND CELL PHYSIOLOGY 36 ( 5 ) 809 - 817 1995.7

Language：English Publisher：JAPANESE SOC PLANT PHYSIOLOGISTS

Activities of phosphatases were found in the fractions which were solubilized from cell walls of both pea and cowpea seedlings with 0.5 M NaCl. These phosphatases hydrolyzed triphosphonucleotides in the order: UTP = CTP > GTP > ATP; and UTP = GTP > CTP = ATP, respectively. The activities of a pyrophosphatase and a p-nitrophenylphosphatase were also detected in these fractions. The suppressor in the spore germination fluid of a pea pathogen, Mycosphaerella pinodes, inhibited all of these phosphatase activities in the fraction solubilized from pea cell walls, but it rather enhanced only the activity of the ATPase among those phosphatases from the cowpea cell wall. Hydrolysis of ATP by a cell wall fraction of pea was also markedly inhibited by the suppressor, while hydrolysis of ATP by similar fractions from cowpea, kidney bean and soybean were rather enhanced by the suppressor, as well as by the elicitor. Thus, the cell wall-bound ATPases responded to the suppressor species-specifically. These cell wall-bound ATPases seemed to be different from the plasma membrane ATPases in several respects. The results suggest that plants recognize the fungal signals not only on their plasma membranes but also on their cell walls and, moreover that putative receptors for the fungal signals might be located close to cell wall-bound ATPases or might even be these ATPases themselves.

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PLANT-LECTINS INDUCE THE PRODUCTION OF A PHYTOALEXIN IN PISUM-SATIVUM

K TOYODA, K MIKI, Y ICHINOSE, T YAMADA, T SHIRAISHI

PLANT AND CELL PHYSIOLOGY 36 ( 5 ) 799 - 807 1995.7

Language：English Publisher：JAPANESE SOC PLANT PHYSIOLOGISTS

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SPECIFIC-INHIBITION OF CELL WALL-BOUND ATPASES BY FUNGAL SUPPRESSOR FROM MYCOSPHAERELLA-PINODES

A KIBA, K TOYODA, Y ICHINOSE, T YAMADA, T SHIRAISHI

PLANT AND CELL PHYSIOLOGY 36 ( 5 ) 809 - 817 1995.7

Language：English Publisher：JAPANESE SOC PLANT PHYSIOLOGISTS

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ESTABLISHMENT OF A SYSTEM FOR THE TRANSIENT EXPRESSION OF GUS GENE IN ELECTROPORATED MUSKMELON (CUCUMIS-MELO L) PROTOPLASTS

SH TAN, NM SALEH, ZC ALANG, T YAMADA, Y ICHINOSE, K KAWAZU

ASIA-PACIFIC JOURNAL OF MOLECULAR BIOLOGY AND BIOTECHNOLOGY 3 ( 2 ) 156 - 160 1995.6

Language：English Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：MALAYSIAN SOC MOLECULAR BIOLOGY BIOTECHNOLOGY

The establishment of a system to isolate protoplasts and introduce foreign gene provides an essential tool in the study of gene expression in crop plants. In electroporation several factors such as pulse strength, pulse length and the amount of plasmid DNA used affect the transient expression of a reporter gene in muskmelon protoplasts. In this study, optimal conditions for electroporation of muskmelon protoplasts were determined to be a single pulse of 3.0 kV/cm pulse strength, 10.0 mu s pulse length and 25.0 mu g of plasmid DNA on a square wave pulse electroporator.

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A SUPPRESCIN FROM A PHYTOPATHOGENIC FUNGUS DEACTIVATES TRANSCRIPTION OF A PLANT DEFENSE GENE ENCODING PHENYLALANINE AMMONIA-LYASE

M WADA, H KATO, K MALIK, P SRIPRASERTSAK, Y ICHINOSE, T SHIRAISHI, T YAMADA

JOURNAL OF MOLECULAR BIOLOGY 249 ( 3 ) 513 - 519 1995.6

Language：English Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：ACADEMIC PRESS (LONDON) LTD

Both elicitor and supprescin (suppressor) are present in the pycnospore germination fluid of a pea pathogen Mycospharella pinodes. A nuclear run-on assay revealed that supprescin rapidly deactivated elicitor-triggered transcription of the gene encoding phenylalanine ammonia-lyase in pea epicotyl tissues. The mechanism underlying the deactivation of the plant defense gene by signal molecules secreted from the fungal pathogen was investigated. Cis-acting sequences and trans-acting factors responsive to supprescin in a TATA-proximal region of a member of the phenylalanine ammonia-lyase gene family in pea were examined in vitro. Gel mobility-shift assays and DNase I footprinting analysis revealed that the promoter region of PSPAL2 was modified by the binding of nuclear factors at multiple sites that were possibly involved in supprescin-mediated deactivation. The prominent changes by supprescin were observed at boxes 2 and 4 and near exonic sequences.

DOI： 10.1006/jmbi.1995.0313

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CHARACTERIZATION OF NUCLEAR FACTORS FOR ELICITOR-MEDIATED ACTIVATION OF THE PROMOTER OF THE PEA PHENYLALANINE AMMONIA-LYASE GENE

H KATO, M WADA, K MURAYA, K MALIK, T SHIRAISHI, Y ICHINOSE, T YAMADA

PLANT PHYSIOLOGY 108 ( 1 ) 129 - 139 1995.5

Language：English Publisher：AMER SOC PLANT PHYSIOLOGISTS

The nuclear factors presumably associated with the activation of the gene encoding phenylalanine ammonia-lyase by a fungal elicitor were characterized in pea (Pisum sativum L.) epicotyls. The TATA-proximal region was dissected and putative cis-regulatory elements in the promoter of pea phenylalanine ammonia-lyase gene 1 were examined by gel-mobility shift and in vitro footprinting analyses. Specific binding of the nuclear factors to the promoter-proximal regions of pea phenylalanine ammonia-lyase gene 1 associated with elicitor-mediated activation was detected at a region containing consensus sequence motifs of boxes 2 and 4 and other AT-rich sequences. The analyses of DNA fragments containing the deleted promoter regions suggested that a residue from -183 to -173 (ATTAGTAAGTGAT) was essential for a maximal activity of forming low-mobility complex (LMC) in the gel-mobility shift assay, and synthetic oligonucleotides confirmed the presence of at least one nuclear component associated with the formation of an active LMC. Competition experiments and treatment with Hoechst 33258 provided direct evidence that the formation of LMC with the promoter fragments from genes encoding phenylalanine ammonia-lyase and chalcone synthase in pea contained one or more of the same proteins that recognize AT-rich sequence motifs for binding. It also suggests that common high-mobility group-like proteins might be involved in the regulation of elicitor-inducible genes in pea.

DOI： 10.1104/pp.108.1.129

RELATIONSHIP BETWEEN DEFENSE RESPONSESAND ION FLUX

AMANO Masashi, TOYODA Kazuhiro, ICHINOSE Yuki, YAMADA Tetsuji, SHIRAISHI Tomonori

36 S119 1995.3

TRANSCRIPTIONAL REGULATION OF THE GENEENCODING CHALCONE SYNTHASE IN PEA BY FUNGAL ELICITOR

SEKI Hikaru, ICHINOSE Yuki, SHIRAISHI Tomonori, YAMADA Tetsuji

36 S120 1995.3

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