Identification of a Basic Glycoprotein Induced by Ethylene in Primary Leaves of Azuki Bean as a Cationic Peroxidase

Ishige, Fumiharu; Mori, Hideo; Yamazaki, Kana; Imaseki, Hidemasa

doi:10.1104/pp.101.1.193

Cited by 39 publications

(11 citation statements)

References 21 publications

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“…Analysis of the purified chitinases by NaDodSO4/polyacrylamide gel electrophoresis showed single bands with apparent molecular mass values of =30 kDa (Fig. 3), similar to the size of ethylene-induced chitinases from bean leaves (20), pea pods (21), and azuki bean leaves (25). Differently substituted Nod factors from R. sp.…”

mentioning

confidence: 58%

Perception of Rhizobium nodulation factors by tomato cells and inactivation by root chitinases.

Staehelin

Granado²,

Müller³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

176

118

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mentioning

confidence: 58%

Perception of Rhizobium nodulation factors by tomato cells and inactivation by root chitinases.

Staehelin

Granado²,

Müller³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

176

118

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“…Previous reports on peroxidases point in this direction [20,28,33,36,38]. In this case, the expression of TPX1 could be similar to the salt-induced expression of the osmotin gene in tobacco, which is regulated by at least eight hormonal and environmental signals, including ABA, ethylene, tobacco mosaic virus, salinity, water deficit, ultraviolet light, wounding and fungal infection [25].…”

Section: Southern Analysismentioning

confidence: 86%

Characterization and in situ localization of a salt-induced tomato peroxidase mRNA

et al. 1994

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NaCl treatment of tomato plants in hydroponic culture at concentrations as low as 50 mM resulted in enhanced accumulation of transcripts of TPX1, a full-length cDNA clone that we had isolated from a library of NaCl-treated tomato plants using a peroxidase-specific oligonucleotide probe. Although the overall amino acid sequence identity of TPX1 to other peroxidase genes was less than 45%, there was a very high degree of identity in all of the conserved domains. The deduced amino acid sequence included the presence of a N-terminal signal peptide but not the C-terminal extension present in peroxidases targeted to the vacuole. The mature protein has a theoretical pI value of 7.5. Transcripts that hybridized to TPX1 were detected only in the roots with higher levels of mRNA in epidermal and subepidermal cell layers. Isoelectric focusing of root extracts showed two major bands of peroxidase activity at pI 5.9 and 6.2. Both activities increased with salt treatment. Southern analysis indicated the presence of only a single TPX1 gene in tomato.

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“…It also participates in the oxidation of phenolic compounds that accumulate in response to infection by pathogens (Van Loon et al, 2006) and activates plant defence genes (F€ urstenberg-H€ agg et al 2013). Furthermore, POX participates in the biosynthesis of ethylene plant hormones, the oxidation of phenolic compounds that accumulate in infection responses, the oxidation of indole-3-acetic acid (IAA) and lignin biosynthesis (Ishige et al 1993). Howell et al (2000) treated seeds with T. virens and found a stimulus in the defence response of cotton roots against R. solani, with increases in terpenoids synthesis and POX activity.…”

Section: Discussionmentioning

confidence: 99%

Trichoderma aureoviride URM 5158 and Trichoderma hamatum URM 6656 are Biocontrol Agents that act against Cassava Root rot through different Mechanisms

Silva

Medeiros

Silva

et al. 2016

Journal of Phytopathology

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Trichoderma has been used to manage a large number of pathogens, but there is a gap in the mechanisms used by these biocontrol agents regarding the physiological response of cassava plants (Manihot esculenta) when it is subjected to cassava root rot. The aims of this study were to investigate the antagonist activity of ten Trichoderma isolates against Fusarium solani on potato dextrose Agar (PDA), to quantify the chitinase production, to select and test in vivo the best isolate from each experiment and to assess the physiological response of cassava to the production of oxidative enzyme complex production (ascorbate peroxidase, catalase, peroxidase and polyphenol oxidase). All Trichoderma isolates have shown competitive capability against F. solani, and Trichoderma hamatum URM 6656 showed the highest inhibition of pathogen growth (88.91%). All isolates have shown chitinase activity, but Trichoderma aureoviride URM 5158 produced the highest amount of chitinase. T. hamatum URM 6656 and T. aureoviride URM 5158 were selected to be applied in vivo. The two Trichoderma strains reduced 64 and 60% of the disease severity in the shoot and 82 and 84% in the root. Cassava plants infected with Trichoderma have shown the highest peroxidase and ascorbate peroxidase production. Our results have indicated that T. aureoviride URM 5158 is an effective biocontrol agent against cassava root rot caused by F. solani, because it presented competitive antagonist capability in vitro, the highest chitinase production, and reduced the cassava root rot severity. The application of T. aureoviride has led to the maximum enzyme activity of reactive oxygen species group in cassava plants.

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Identification of a Basic Glycoprotein Induced by Ethylene in Primary Leaves of Azuki Bean as a Cationic Peroxidase

Cited by 39 publications

References 21 publications

Perception of Rhizobium nodulation factors by tomato cells and inactivation by root chitinases.

Perception of Rhizobium nodulation factors by tomato cells and inactivation by root chitinases.

Characterization and in situ localization of a salt-induced tomato peroxidase mRNA

Trichoderma aureoviride URM 5158 and Trichoderma hamatum URM 6656 are Biocontrol Agents that act against Cassava Root rot through different Mechanisms

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