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

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 signali...

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Main Authors: Kovacs, Izabella (Author) , Holzmeister, Christian (Author) , Wirtz, Markus (Author) , Geerlof, Arie (Author) , Fröhlich, Thomas (Author) , Römling, Gaby (Author) , Kuruthukulangarakoola, Gitto T. (Author) , Linster, Eric (Author) , Hell, Rüdiger (Author) , Arnold, Georg J. (Author) , Durner, Jörg (Author) , Lindermayr, Christian (Author)
Format: Article (Journal)
Language:English
Published: 10 November 2016
In: Frontiers in plant science
Year: 2016, Volume: 7, Pages: 1-17
ISSN:1664-462X
DOI:10.3389/fpls.2016.01669
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.3389/fpls.2016.01669
Verlag, lizenzpflichtig, Volltext: https://www.frontiersin.org/articles/10.3389/fpls.2016.01669/full
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Author Notes: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
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Summary: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.
Item Description:Gesehen am 25.05.2020
Physical Description:Online Resource
ISSN:1664-462X
DOI:10.3389/fpls.2016.01669

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