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Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues.
Biochem Biophys Res Commun. 2017 12 09; 494(1-2):27-33.BB

Abstract

Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible S-nitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO- donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode.

Authors+Show Affiliations

Department of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, CZ-783 71 Olomouc, Czech Republic.Department of Biochemistry, Faculty of Science, Masaryk University, Kamenice 753/5, CZ-625 00 Brno, Czech Republic.Department of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, CZ-783 71 Olomouc, Czech Republic.Department of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, CZ-783 71 Olomouc, Czech Republic.Department of Biochemistry, Faculty of Science, Palacký University, Šlechtitelů 27, CZ-783 71 Olomouc, Czech Republic. Electronic address: marek.petrivalsky@upol.cz.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

29061305

Citation

Tichá, Tereza, et al. "Redox Regulation of Plant S-nitrosoglutathione Reductase Activity Through Post-translational Modifications of Cysteine Residues." Biochemical and Biophysical Research Communications, vol. 494, no. 1-2, 2017, pp. 27-33.
Tichá T, Lochman J, Činčalová L, et al. Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues. Biochem Biophys Res Commun. 2017;494(1-2):27-33.
Tichá, T., Lochman, J., Činčalová, L., Luhová, L., & Petřivalský, M. (2017). Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues. Biochemical and Biophysical Research Communications, 494(1-2), 27-33. https://doi.org/10.1016/j.bbrc.2017.10.090
Tichá T, et al. Redox Regulation of Plant S-nitrosoglutathione Reductase Activity Through Post-translational Modifications of Cysteine Residues. Biochem Biophys Res Commun. 2017 12 9;494(1-2):27-33. PubMed PMID: 29061305.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues. AU - Tichá,Tereza, AU - Lochman,Jan, AU - Činčalová,Lucie, AU - Luhová,Lenka, AU - Petřivalský,Marek, Y1 - 2017/10/21/ PY - 2017/10/13/received PY - 2017/10/17/accepted PY - 2017/10/25/pubmed PY - 2017/11/14/medline PY - 2017/10/25/entrez KW - Nitric oxide KW - Post-translational modifications KW - Redox regulation KW - S-nitrosation KW - S-nitrosoglutathione reductase SP - 27 EP - 33 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 494 IS - 1-2 N2 - Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible S-nitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO- donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/29061305/Redox_regulation_of_plant_S_nitrosoglutathione_reductase_activity_through_post_translational_modifications_of_cysteine_residues_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(17)32068-5 DB - PRIME DP - Unbound Medicine ER -