Stress response of NAD+-dependent formate dehydrogenase in Gossypium hirsutum L. grown under copper toxicity

Abstract

Cotton (Gossypium hirsutum L.), which is not directly involved in the food chain, appears to be a suitable candidate to remove heavy metals from the food chain and to be a commercial plant which could be planted in contaminated soils. The key point of this approach is selection of the right genotype, which has heavy metal resistance or hyperaccumulation properties. Therefore, in the present study, two G. hirsutum genotypes, Erşan-92 and N-84S, were grown under copper stress and investigated to obtain further insights about the heavy metal tolerance mechanisms of plants by focusing on the expression of NAD-dependent formate dehydrogenase (FDH). In accordance with the results, which were obtained from RT-PCR analysis and activity measurements, in the Erşan-92 root tissue, FDH activity increased significantly with increasing metal concentrations and a 6.35-fold higher FDH activity was observed in the presence of 100-μM Cu. As opposed to Erşan-92, the maximum FDH activity in the roots of N-84S, which were untreated with copper as the control plants, was measured as 0.0141-U mg g FW, and the activity decreased significantly with the increasing metal concentrations. The metallothionein (GhMT3a) transcript level of the plants grown in a medium containing different Cu concentrations showed nearly the same pattern as that of the FDH gene transcription. It was observed that while the tolerance of N-84S in the lower Cu concentration reduces remarkably, Erşan-92 continues to struggle up to 100-μM Cu. The results of the SOD analysis also confirm this activity of Erşan-92 against the Cu stress.

Thermopriming-associated proteome and sugar content responses in Pinus radiata embryogenic tissue

“…Even if most of them presented a down-regulation tendency, such as ubiquinol oxidase 1a, whose function as alternative oxidase is known to be important during both biotic and abiotic stress (Vanlerberghe, 2013), three proteins were up-regulated in response to heat: formate dehydrogenase, thioredoxin H-type and glutathione S-transferase DHAR3. As previously mentioned, formate dehydrogenase is a universal stress protein involved in the responses to various abiotic and biotic stresses by catalysing the oxidation of formate, a byproduct of ROS scavenging, and maintaining a reducing environment in the cell (Kurt-Gür et al, 2018). Several studies have demonstrated that heat can induce the synthesis of this enzyme (Ren et al, 2019) and its abundance seems to be regulated by the 26S proteasome (McNeilly et al, 2018).…”

Long non-coding RNAs and their potential function in response to postharvest senescence of Sparassis latifolia during cold storage

“…Formate dehydrogenases (FDH) are a group of enzymes that catalyze the oxidation of formate to carbon dioxide, which are also involved in energetic metabolism and pathways related to stress response 38 . The FDH activity increased significantly with increasing copper concentrations to help cotton scope with copper toxicity 39 . Under hypoxic stress, FDH activity is significantly increased in the potato tubers 40 .…”

Involvement of SlSTOP1 regulated SlFDH expression in aluminum tolerance by reducing NAD+ to NADH in the tomato root apex

“…The colorimetric assay was performed using 200 m m sodium phosphate (pH 7.5) containing 0.4 mg ml −1 nitroblue tetrazolium (NBT) and 0.03 mg ml −1 PMS with or without 2 μg recombinant protein, 1.62 m m NAD + and 162 m m formate (Kurt‐Gür et al., 2018). In this assay, NBT receives electrons from NADH via PMS and generates blue‐purple formazan.…”