Stress-Induced Detoxification Enzymes in Rice Have Broad Substrate Affinity

Abstract

Reactive carbonyl compounds (RCCs) such as hydroxynonenol, malondialdehyde, acrolein, crotonaldehyde, methylglyoxal, and glyoxal accumulate at higher levels under stress in plants and damage the cell metabolic activities. Plants have evolved several detoxifying enzymes such as aldo-keto reductases (AKRs), aldehyde/alcohol dehydrogenases (ALDH/ADH), and glyoxalases. We report the phylogenetic relationship of these proteins and in silico analysis of rice-detoxifying protein structures and their substrate affinity with cofactors using docking and molecular simulation studies. Molecular simulations with nicotinamide adenine dinucleotide phosphate or glutathione cofactor docking with commonly known reactive substrates suggests that the AKRs, ALDH, and ADH proteins attain maximum conformational changes, whereas glyoxalase has fewer conformational changes with cofactor binding. Several AKRs showed a significant binding affinity with many RCCs. The rice microarray studies showed enhanced expression of many AKRs in resistant genotypes, which also showed higher affinity to RCCs, signifying their importance in managing carbonyl stress. The higher expression of AKRs is regulated by stress-responsive transcription factors (TFs) as we identified stress-specific cis-elements in their promoters. The study reports the stress-responsive nature of AKRs, their regulatory TFs, and their best RCC targets, which may be used for crop improvement programs.