Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
29061305
DOI
10.1016/j.bbrc.2017.10.090
PII: S0006-291X(17)32068-5
Knihovny.cz E-resources
- Keywords
- Nitric oxide, Post-translational modifications, Redox regulation, S-nitrosation, S-nitrosoglutathione reductase,
- MeSH
- Aldehyde Oxidoreductases antagonists & inhibitors chemistry metabolism MeSH
- Cysteine chemistry metabolism MeSH
- Nitric Oxide Donors pharmacology MeSH
- Nitrosation MeSH
- Nitric Oxide metabolism MeSH
- Oxidation-Reduction MeSH
- Hydrogen Peroxide pharmacology MeSH
- Protein Processing, Post-Translational MeSH
- Recombinant Proteins chemistry genetics metabolism MeSH
- Plant Proteins antagonists & inhibitors chemistry metabolism MeSH
- S-Nitrosoglutathione metabolism MeSH
- S-Nitrosothiols metabolism MeSH
- Signal Transduction MeSH
- Solanum lycopersicum genetics growth & development metabolism MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Aldehyde Oxidoreductases MeSH
- Cysteine MeSH
- Nitric Oxide Donors MeSH
- formaldehyde dehydrogenase, glutathione-independent MeSH Browser
- Nitric Oxide MeSH
- Hydrogen Peroxide MeSH
- Recombinant Proteins MeSH
- Plant Proteins MeSH
- S-Nitrosoglutathione MeSH
- S-Nitrosothiols MeSH
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.
References provided by Crossref.org
Thioredoxins: Emerging Players in the Regulation of Protein S-Nitrosation in Plants
Signaling Toward Reactive Oxygen Species-Scavenging Enzymes in Plants
S-Nitrosoglutathione Reductase-The Master Regulator of Protein S-Nitrosation in Plant NO Signaling
