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Identification of nuclear target proteins for S-nitrosylation in pathogen-treated Arabidopsis thaliana cell cultures.

Plant Sci. 238, 115-126 (2015)
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Nitric oxide (NO) is a significant signalling molecule involved in the regulation of many different physiological processes in plants. One of the most imperative regulatory modes of action of NO is protein S-nitrosylation—the covalent attachment of an NO group to the sulfur atom of cysteine residues. In this study, we focus on S-nitrosylation of Arabidopsis nuclear proteins after pathogen infection. After treatment of Arabidopsis suspension cell cultures with pathogens, nuclear proteins were extracted and treated with the S-nitrosylating agent S-nitrosoglutathione (GSNO). A biotin switch assay was performed and biotin-labelled proteins were purified by neutravidin affinity chromatography and identified by mass spectrometry. A total of 135 proteins were identified, whereas nuclear localization has been described for 122 proteins of them. 117 of these proteins contain at least one cysteine residue. Most of the S-nitrosylated candidates were involved in protein and RNA metabolism, stress response, and cell organization and division. Interestingly, two plant-specific histone deacetylases were identified suggesting that nitric oxide regulated epigenetic processes in plants. In sum, this work provides a new collection of targets for protein S-nitrosylation in Arabidopsis and gives insight into the regulatory function of NO in the nucleus during plant defense response. Moreover, our data extend the knowledge on the regulatory function of NO in events located in the nucleus.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Nitric oxide; Post-translational modification; Protein S-nitrosylation; Biotin switch technique; Cysteine residues; Plant defense response; Histone Deacetylase Hd2; Oxide Synthase Activity; Heat-shock-protein; Nitric-oxide; Proteomic Identification; Transcription Factor; Gene-transcription; Reactive Nitrogen; Redox Regulation; Cold Stress
ISSN (print) / ISBN 0168-9452
e-ISSN 0168-9452
Zeitschrift Plant Science
Quellenangaben Band: 238, Heft: , Seiten: 115-126 Artikelnummer: , Supplement: ,
Verlag Elsevier
Verlagsort Clare
Begutachtungsstatus Peer reviewed