Effect of Salt Stress on the Expression and Promoter Methylation of the Genes Encoding the Mitochondrial and Cytosolic Forms of Aconitase and Fumarase in Maize.

The influence of salt stress on gene expression, promoter methylation, and enzymatic activity of the mitochondrial and cytosolic forms of aconitase and fumarase has been investigated in maize (Zea mays L.) seedlings. The incubation of maize seedlings in 150-mM NaCl solution resulted in a several-fold increase of the mitochondrial activities of aconitase and fumarase that peaked at 6 h of NaCl treatment, while the cytosolic activity of aconitase and fumarase decreased. This corresponded to the decrease in promoter methylation of the genes Aco1 and Fum1 encoding the mitochondrial forms of these enzymes and the increase in promoter methylation of the genes Aco2 and Fum2 encoding the cytosolic forms. The pattern of expression of the genes encoding the mitochondrial forms of aconitase and fumarase corresponded to the profile of the increase of the stress marker gene ZmCOI6.1. It is concluded that the mitochondrial and cytosolic forms of aconitase and fumarase are regulated via the epigenetic mechanism of promoter methylation of their genes in the opposite ways in response to salt stress. The role of the mitochondrial isoforms of aconitase and fumarase in the elevation of respiration under salt stress is discussed.

Regulation of expression of the mitochondrial and cytosolic forms of aconitase in maize leaves via phytochrome.

Regulation of expression and methylation of promoters of two aconitase (EC 4.2.1.3) genes by light have been investigated in maize (Zea mays L.) in relation to the involvement of phytochrome. Transferring of plants from light to darkness resulted in the stimulation of aconitase activity in mitochondria and in its suppression in the cytosol. Irradiation by red light reversed aconitase activity to the levels observed under white light while far red light reverted the effect of red light. Electrophoretic staining of aconitase activity revealed the preference of the cytosolic form in white and red light and of the mitochondrial form in darkness and in far red light. Both forms of aconitase were purified, the mitochondrial form revealed lower affinity to citrate and higher to isocitrate as compared to the cytosolic form. The study of the aconitase gene Aco1 encoding the mitochondrial form revealed its low expression and high promoter methylation in the light and upon irradiation by red light as compared to high expression and low promoter methylation in darkness and in far red light. The pattern of expression and promoter methylation of the gene Aco2 encoding the cytosolic form was opposite. It is concluded that expression of the mitochondrial and cytosolic forms of aconitase is under control of light via phytochrome in opposite ways at the level of promoter methylation. Light inhibits expression of the mitochondrial aconitase, while it stimulates expression of the cytosolic aconitase which is important for directing citrate exported from mitochondria to the synthesis of amino acids.

Expression of succinate dehydrogenase and fumarase genes in maize leaves is mediated by cryptochrome.

Blue light inhibits succinate dehydrogenase and fumarase enzyme activity and gene expression in green leaves of maize (Zea mays L.). Irradiation of maize plants by blue light resulted in the transient decrease of transcripts of genes Sdh1-2 and Sdh2-3 encoding correspondingly the flavoprotein and iron-sulfur protein subunits of succinate dehydrogenase, and of Fum1 encoding the mitochondrial form of fumarase. The blue light effect was probably mediated by transcription factors COP1 and HY5, with the expression of the latter increased upon blue light treatment. This was accompanied by a decrease in the expression of COP1, presumably involved in proteasome degradation of HY5. It was also demonstrated that calcium ions do not participate in this process.