Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i>
Glucosinolates and their degradation products have a wide range of actions and are important components of plant defense. <i>NSP2</i> (nitrile-specific protein 2) is a key regulator in the breakdown process of glucosinolates. However, the precise function of <i>NSP2</i> in pl...
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MDPI AG
2023-08-01
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author | Tingting Zhai Jun Teng Xintong Fan Shaowei Yu Chen Wang Xingqi Guo Wei Yang Shuxin Zhang |
author_facet | Tingting Zhai Jun Teng Xintong Fan Shaowei Yu Chen Wang Xingqi Guo Wei Yang Shuxin Zhang |
author_sort | Tingting Zhai |
collection | DOAJ |
description | Glucosinolates and their degradation products have a wide range of actions and are important components of plant defense. <i>NSP2</i> (nitrile-specific protein 2) is a key regulator in the breakdown process of glucosinolates. However, the precise function of <i>NSP2</i> in plant disease resistance beyond its role in glucosinolate degradation is still unclear. In this study, we discovered that <i>NSP2</i> which was induced by <i>Pst</i> DC3000, influenced <i>PR</i> genes expression and reactive oxygen burst. Additionally, omics analysis revealed that NSP2 was engaged in plant-pathogen interaction and several hormone signal transduction pathways. Furthermore, immunoprecipitation-tandem mass spectrometry analysis (IP-MS), bimolecular fluorescence complementation (BiFC), and co-immunoprecipitation demonstrated that NSP2 interacts with MPK3. Genetic analysis shows that <i>NSP2</i> may be a function downstream of <i>MPK3</i>. Upon pathogen inoculation, NSP2 protein levels increase while MPK3 protein levels decrease. Moreover, the level of phosphorylated NSP2 decreases. Taken together, this study sheds light on a new mode of synergistic action between NSP2 and MPK3 in the disease resistance process. |
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spelling | doaj.art-65e752958bef4fc8862ebc56eab315c32023-11-18T23:26:50ZengMDPI AGPlants2223-77472023-08-011215285710.3390/plants12152857Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i>Tingting Zhai0Jun Teng1Xintong Fan2Shaowei Yu3Chen Wang4Xingqi Guo5Wei Yang6Shuxin Zhang7National Key Laboratory of Wheat Improvement, College of Life Science, Shandong Agricultural University, Tai’an 271018, ChinaCollege of Animal Science and Technology, Shandong Agricultural University, Tai’an 271018, ChinaNational Key Laboratory of Wheat Improvement, College of Life Science, Shandong Agricultural University, Tai’an 271018, ChinaNational Key Laboratory of Wheat Improvement, College of Life Science, Shandong Agricultural University, Tai’an 271018, ChinaNational Key Laboratory of Wheat Improvement, College of Life Science, Shandong Agricultural University, Tai’an 271018, ChinaSchool of Chemical and Biological Engineering, Qilu Institute of Technology, Jinan 271018, ChinaNational Key Laboratory of Wheat Improvement, College of Life Science, Shandong Agricultural University, Tai’an 271018, ChinaNational Key Laboratory of Wheat Improvement, College of Life Science, Shandong Agricultural University, Tai’an 271018, ChinaGlucosinolates and their degradation products have a wide range of actions and are important components of plant defense. <i>NSP2</i> (nitrile-specific protein 2) is a key regulator in the breakdown process of glucosinolates. However, the precise function of <i>NSP2</i> in plant disease resistance beyond its role in glucosinolate degradation is still unclear. In this study, we discovered that <i>NSP2</i> which was induced by <i>Pst</i> DC3000, influenced <i>PR</i> genes expression and reactive oxygen burst. Additionally, omics analysis revealed that NSP2 was engaged in plant-pathogen interaction and several hormone signal transduction pathways. Furthermore, immunoprecipitation-tandem mass spectrometry analysis (IP-MS), bimolecular fluorescence complementation (BiFC), and co-immunoprecipitation demonstrated that NSP2 interacts with MPK3. Genetic analysis shows that <i>NSP2</i> may be a function downstream of <i>MPK3</i>. Upon pathogen inoculation, NSP2 protein levels increase while MPK3 protein levels decrease. Moreover, the level of phosphorylated NSP2 decreases. Taken together, this study sheds light on a new mode of synergistic action between NSP2 and MPK3 in the disease resistance process.https://www.mdpi.com/2223-7747/12/15/2857<i>NSP2</i><i>MPK3</i><i>Pst</i> DC3000phosphorylationdisease resistance |
spellingShingle | Tingting Zhai Jun Teng Xintong Fan Shaowei Yu Chen Wang Xingqi Guo Wei Yang Shuxin Zhang Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i> Plants <i>NSP2</i> <i>MPK3</i> <i>Pst</i> DC3000 phosphorylation disease resistance |
title | Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i> |
title_full | Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i> |
title_fullStr | Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i> |
title_full_unstemmed | Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i> |
title_short | Nitrile-Specific Protein NSP2 and Its Interacting Protein MPK3 Synergistically Regulate Plant Disease Resistance in <i>Arabidopsis</i> |
title_sort | nitrile specific protein nsp2 and its interacting protein mpk3 synergistically regulate plant disease resistance in i arabidopsis i |
topic | <i>NSP2</i> <i>MPK3</i> <i>Pst</i> DC3000 phosphorylation disease resistance |
url | https://www.mdpi.com/2223-7747/12/15/2857 |
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