4.7 Article

Redox Regulation of Salt Tolerance in Eutrema salsugineum by Proteomics

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MDPI
DOI: 10.3390/ijms241914518

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Eutrema salsugineum; NaCl; TMT; redox proteomics; glutathione peroxidase

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Salt stress can cause changes in redox modifications, which affect cell redox homeostasis and protein function. Eutrema salsugineum, a halophytic plant, has been used to study the role of redox modifications and signaling pathways in response to salt stress. This research provides a foundation for understanding the molecular mechanisms of plant salt response.
Salt stress severely restricts plant growth and crop production, which is accompanied by accumulation of reactive oxygen species (ROS) that disturb cell redox homeostasis and oxidize redox-sensitive proteins. Eutrema salsugineum, a halophytic species closely related to Arabidopsis, shows a high level of tolerance to salinity and is increasingly used as a model plant in abiotic stress biology. To understand redox modifications and signaling pathways under salt stress, we used tandem mass tag (TMT)-based proteomics to quantify the salt-induced changes in protein redox modifications in E. salsugineum. Salt stress led to increased oxidative modification levels of 159 cysteine sites in 107 proteins, which play roles in carbohydrate and energy metabolism, transport, ROS homeostasis, cellular structure modulation, and folding and assembly. These lists of unknown redox reactive proteins in salt mustard lay the foundation for future research to understand the molecular mechanism of plant salt response. However, glutathione peroxidase (GPX) is one of the most important antioxidant enzymes in plants. Our research indicates that EsGPX may be involved in regulating ROS levels and that plants with overexpressed EsGPX have much improved salt tolerance.

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