ROS-mediated inhibition of S-nitrosoglutathione reductase contributes to the activation of anti-oxidative mechanisms

• Verfasst von: Kovacs, Izabella [VerfasserIn]
• Verfasst von: Holzmeister, Christian [VerfasserIn]
• Verfasst von: Wirtz, Markus [VerfasserIn]
• Verfasst von: Geerlof, Arie [VerfasserIn]
• Verfasst von: Fröhlich, Thomas [VerfasserIn]
• Verfasst von: Römling, Gaby [VerfasserIn]
• Verfasst von: Kuruthukulangarakoola, Gitto T. [VerfasserIn]
• Verfasst von: Linster, Eric [VerfasserIn]
• Verfasst von: Hell, Rüdiger [VerfasserIn]
• Verfasst von: Arnold, Georg J. [VerfasserIn]
• Verfasst von: Durner, Jörg [VerfasserIn]
• Verfasst von: Lindermayr, Christian [VerfasserIn]
• Titel: ROS-mediated inhibition of S-nitrosoglutathione reductase contributes to the activation of anti-oxidative mechanisms
• Verf.angabe: Izabella Kovacs, Christian Holzmeister, Markus Wirtz, Arie Geerlof, Thomas Fröhlich, Gaby Römling, Gitto T. Kuruthukulangarakoola, Eric Linster, Rüdiger Hell, Georg J. Arnold, Jörg Durner and Christian Lindermayr
• E-Jahr: 2016
• Jahr: 10 November 2016
• Umfang: 17 S.
• Fussnoten: Gesehen am 25.05.2020
• Titel Quelle: Enthalten in: Frontiers in plant science
• Ort Quelle: Lausanne : Frontiers Media, 2010
• Jahr Quelle: 2016
• Band/Heft Quelle: 7(2016), Seite 1-17
• ISSN Quelle: 1664-462X
• DOI: doi:10.3389/fpls.2016.01669
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Arabidopsis thaliana
• Sach-SW: Hydrogen Peroxide
• Sach-SW: Nitric Oxide
• Sach-SW: Oxidative Stress
• Sach-SW: Paraquat
• Sach-SW: Reactive Oxygen Species
• Sach-SW: S-nitrosoglutathione reductase
• Sach-SW: S-Nitrosothiols
• K10plus-PPN: 1698740093

Abstract

Nitric oxide (NO) has emerged as a signaling molecule in plants being involved in diverse physiological processes like germination, root growth, stomata closing and response to biotic and abiotic stress. S-nitrosoglutathione (GSNO) as a biological NO donor has a very important function in NO signaling since it can transfer its NO moiety to other proteins (trans-nitrosylation). Such trans-nitrosylation reactions are equilibrium reactions and depend on GSNO level. The breakdown of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme controls S-nitrosothiol levels and regulates NO signaling. Here we report that Arabidopsis thaliana GSNOR activity is reversibly inhibited by H2O2 in-vitro and by paraquat-induced oxidative stress in-vivo. Light scattering analyses of reduced and oxidized recombinant GSNOR demonstrated that GSNOR proteins form dimers under both reducing and oxidizing conditions. Moreover, mass spectrometric analyses revealed that H2O2-treatment increased the amount of oxidative modifications on Zn2+-coordinating Cys47 and Cys177. Inhibition of GSNOR results in enhanced levels of S-nitrosothiols followed by accumulation of glutathione. Moreover, transcript levels of redox-regulated genes and activities of glutathione-dependent enzymes are increased in gsnor-ko plants, which may contribute to the enhanced resistance against oxidative stress. In sum, our results demonstrate that ROS-dependent inhibition of GSNOR is playing an important role in activation of anti-oxidative mechanisms to damping oxidative damage and imply a direct crosstalk between ROS- and NO-signaling.