Short-term low temperature induces nitro-oxidative stress that deregulates the NADP-Malic enzyme function by tyrosine nitration in arabidopsis thaliana
| Autor: | Beatriz Sánchez-Calvo, Juan B. Barroso, Juan C. Begara-Morales, Francisco J. Corpas, Capilla Mata-Pérez, Raquel Valderrama, Mounira Chaki, María V. Gómez-Rodríguez, Javier Lopez-Jaramillo |
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| Přispěvatelé: | Universidad de Jaén, Ministerio de Economía y Competitividad (España), Junta de Andalucía, European Commission |
| Rok vydání: | 2019 |
| Předmět: |
0106 biological sciences
0301 basic medicine NADP malic enzyme Nitro-oxidative stress Physiology Clinical Biochemistry low temperature medicine.disease_cause 01 natural sciences Biochemistry peroxynitrite Peroxynitrite Nitric oxide 03 medical and health sciences chemistry.chemical_compound nitric oxide Nitration medicine Low temperature Tyrosine Molecular Biology Reactive nitrogen species chemistry.chemical_classification reactive oxygen species Reactive oxygen species Superoxide lcsh:RM1-950 fungi food and beverages Cell Biology tyrosine nitration lcsh:Therapeutics. Pharmacology 030104 developmental biology reactive nitrogen species chemistry nitro-oxidative stress Oxidative stress 010606 plant biology & botany |
| Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname Antioxidants Volume 8 Issue 10 Digibug. Repositorio Institucional de la Universidad de Granada Antioxidants, Vol 8, Iss 10, p 448 (2019) |
| Popis: | Low temperature (LT) negatively affects plant growth and development via the alteration of the metabolism of reactive oxygen and nitrogen species (ROS and RNS). Among RNS, tyrosine nitration, the addition of an NO2 group to a tyrosine residue, can modulate reduced nicotinamide-dinucleotide phosphate (NADPH)-generating systems and, therefore, can alter the levels of NADPH, a key cofactor in cellular redox homeostasis. NADPH also acts as an indispensable electron donor within a wide range of enzymatic reactions, biosynthetic pathways, and detoxification processes, which could affect plant viability. To extend our knowledge about the regulation of this key cofactor by this nitric oxide (NO)-related post-translational modification, we analyzed the effect of tyrosine nitration on another NADPH-generating enzyme, the NADP-malic enzyme (NADP-ME), under LT stress. In Arabidopsis thaliana seedlings exposed to short-term LT (4 °C for 48 h), a 50% growth reduction accompanied by an increase in the content of superoxide, nitric oxide, and peroxynitrite, in addition to diminished cytosolic NADP-ME activity, were found. In vitro assays confirmed that peroxynitrite inhibits cytosolic NADP-ME2 activity due to tyrosine nitration. The mass spectrometric analysis of nitrated NADP-ME2 enabled us to determine that Tyr-73 was exclusively nitrated to 3-nitrotyrosine by peroxynitrite. The in silico analysis of the Arabidopsis NADP-ME2 protein sequence suggests that Tyr73 nitration could disrupt the interactions between the specific amino acids responsible for protein structure stability. In conclusion, the present data show that short-term LT stress affects the metabolism of ROS and RNS, which appears to negatively modulate the activity of cytosolic NADP-ME through the tyrosine nitration process. Technical and human support provided by CICT of Universidad de Jaén (UJA, MINECO, Junta de Andalucía, and FEDER) is gratefully acknowledged. |
| Databáze: | OpenAIRE |
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