Jump to Main Content
Modulation of Glycine Betaine Accumulation with Oxidative Stress Induced by Aluminium Toxicity in Rice
- Bera, Subhankar, De, Arnab Kumar, Adak, Malay Kumar
- Proceedings of the National Academy of Sciences, India, Section B: biological sciences 2019 v.89 no.1 pp. 291-301
- aldehyde dehydrogenase, aluminum, betaine, betaine-aldehyde dehydrogenase, cortex, dose response, enzyme activity, gene expression, genes, hydrogen peroxide, oxidative stress, protein synthesis, rice, root growth, superoxide anion, thiols, toxicity
- The present study addresses the sensitivity of rice species to varying concentrations of Al toxicity. Aluminium salt for plants was used in increasing order (240, 360, 480 µM) during short period to decipher the impact of metal stress on metabolic status with reference to oxidative damages. Interestingly, plants responded well with increase in linear root growth. In a dose dependent manner of metal concentration, plants suffered more from developed ROS (both O₂⁻ and H₂O₂) in root cortex. The histochemical detection of tissue lysis as detected by Evans blue and Hematoxylin was in proportionate to the aluminium concentration over control. In response to peroxide radical accumulated in the tissues, plants were characterized in a variable manner for APX, CAT and GR activities. Still, on protein polymorphism of these genes, the plants responded well with a distinct expression varied over control. In support of decreased activity, a single band expression was key feature to characterize the plants under Al toxicity. Plants though maintained a stable proportion of non-thiol content but a steeper up regulation of GR activity at highest concentration of Al was indicating for more GSH recruitment in oxidative stress. Banding patterns of APX, CAT and GR through Al concentrations appeared as bio-indices under metal reactivity in rice species. Betaine aldehyde dehydrogenase was also in proportionate manner to support the synthesis of osmolyte under metal toxicity. This is more relevant with protein expression of aldehyde dehydrogenase activity and distinct bands favor the gene expression under modulation of metal stress.