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<p>A cDNA of VvTrx <i>h</i>4 was isolated from leaf tissue of grape (<i>Vitis vinifera</i> L. cv. Askari) by rapid amplification of cDNA ends (RACE) technique. The VvTrx <i>h</i>4 was heterologously expressed in a bacterial host (<i>Escherichia coli</i>) and its catalytic properties were investigated. The VvTrx <i>h</i>4 showed the disulfide reductase function by reduction of insulin and DTNB as substrates. Under high temperature treatment, the structure of the VvTrx <i>h</i>4 protein was shifted from low molecular weight (LMW) forms to high molecular weight (HMW) species and its disulfide reductase activity subsequently decreased at high temperatures. In addition, the high temperature treatment-dependent structural and functional changes of the VvTrx <i>h</i>4 were induced by treatment with H<sub>2</sub>O<sub>2</sub>. Moreover, further incubation of the VvTrx <i>h</i>4 in H<sub>2</sub>O<sub>2</sub> after elimination of DTT almost returned the oligomeric structures of the VvTrx <i>h</i>4, suggesting that the structural alterations of the VvTrx <i>h</i>4 are affected by redox status. Using protein–protein interaction (PPI) network and molecular docking assays, several target proteins were specified for the VvTrx <i>h</i>4, indicating that the VvTrx <i>h</i>4 is able to provide reducing power for peroxidases (POXs) in order to reduce H<sub>2</sub>O<sub>2</sub> in vitro. Nevertheless, with NADPH-thioredoxin system (NTS), horseradish peroxidase (HRP) catalyzed the reduction of H<sub>2</sub>O<sub>2</sub> more efficiently than glutathione peroxidase (GPX), showing that the VvTrx <i>h</i>4 may act as a regulator for enzymes scavenging reactive oxygen species (ROS). Moreover, the GPX may be indirectly reduced by the NTS pathway through reduced glutathione (GSH), proposing a crosstalk between the NTS and the GSH/GSSG pathways.</p>

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Interaction between a grape thioredoxin h4 and peroxidases: a study based on protein interaction network analysis and experimental validation

  • 期刊论文

  • 发表日期：

    2026年8月4日

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  • Reza Heidari Japelaghi,
  • Raheem Haddad

摘要

A cDNA of VvTrx h4 was isolated from leaf tissue of grape (Vitis vinifera L. cv. Askari) by rapid amplification of cDNA ends (RACE) technique. The VvTrx h4 was heterologously expressed in a bacterial host (Escherichia coli) and its catalytic properties were investigated. The VvTrx h4 showed the disulfide reductase function by reduction of insulin and DTNB as substrates. Under high temperature treatment, the structure of the VvTrx h4 protein was shifted from low molecular weight (LMW) forms to high molecular weight (HMW) species and its disulfide reductase activity subsequently decreased at high temperatures. In addition, the high temperature treatment-dependent structural and functional changes of the VvTrx h4 were induced by treatment with H2O2. Moreover, further incubation of the VvTrx h4 in H2O2 after elimination of DTT almost returned the oligomeric structures of the VvTrx h4, suggesting that the structural alterations of the VvTrx h4 are affected by redox status. Using protein–protein interaction (PPI) network and molecular docking assays, several target proteins were specified for the VvTrx h4, indicating that the VvTrx h4 is able to provide reducing power for peroxidases (POXs) in order to reduce H2O2 in vitro. Nevertheless, with NADPH-thioredoxin system (NTS), horseradish peroxidase (HRP) catalyzed the reduction of H2O2 more efficiently than glutathione peroxidase (GPX), showing that the VvTrx h4 may act as a regulator for enzymes scavenging reactive oxygen species (ROS). Moreover, the GPX may be indirectly reduced by the NTS pathway through reduced glutathione (GSH), proposing a crosstalk between the NTS and the GSH/GSSG pathways.