Phosphoenolpyruvate carboxylase, NADP-malic enzyme, and pyruvate, phosphate dikinase are involved in the acclimation of Nicotiana tabacum L. to drought stress
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
24484954
DOI
10.1016/j.jplph.2013.10.017
PII: S0176-1617(13)00440-9
Knihovny.cz E-resources
- Keywords
- Drought, NADP-malic enzyme, Nicotiana tabacum L., Phosphoenolpyruvate carboxylase, Pyruvate, phosphate dikinase,
- MeSH
- Acclimatization MeSH
- Chloroplasts metabolism MeSH
- Phosphoenolpyruvate Carboxylase genetics metabolism MeSH
- Stress, Physiological physiology MeSH
- Real-Time Polymerase Chain Reaction MeSH
- Plant Leaves enzymology MeSH
- Malate Dehydrogenase genetics metabolism MeSH
- Droughts * MeSH
- Pyruvate, Orthophosphate Dikinase genetics metabolism MeSH
- Gene Expression Regulation, Plant MeSH
- Plant Proteins genetics metabolism MeSH
- Nicotiana enzymology genetics MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Phosphoenolpyruvate Carboxylase MeSH
- Malate Dehydrogenase MeSH
- malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) MeSH Browser
- Pyruvate, Orthophosphate Dikinase MeSH
- Plant Proteins MeSH
Drought stress is one of the most frequent forms of abiotic stresses, which occurs under condition of limited water availability. In this work, the possible participation of phosphoenolpyruvate carboxylase (EC 4.1.1.31; PEPC), NADP-malic enzyme (EC 1.1.1.40; NADP-ME), and pyruvate, phosphate dikinase (EC 2.7.9.1; PPDK) in response to drought of tobacco plants (Nicotiana tabacum L., cv. W38) was investigated. Enzyme specific activities in tobacco leaves of drought stressed plants were significantly increased after 11 days of stress, PEPC 2.3-fold, NADP-ME 3.9-fold, and PPDK 2.7-fold compared to control plants. The regulation of PEPC and NADP-ME activities were studied on transcriptional level by the quantitative RT PCR and on translational level - immunochemically. The amount of NADP-ME protein and transcription of mRNA for chloroplastic NADP-ME isoform were increased indicating their enhanced synthesis de novo. On the other hand, mRNA for cytosolic isoform of NADP-ME was decreased. The changes in PEPC protein and PEPC mRNA were not substantial. Therefore regulation of PEPC activity by phosphorylation was evaluated and found to be involved in the stress response. During recovery, activities of the tested enzymes returned close to their basal levels.
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