Browsing by Author "Chatterjee, Yajnaseni"

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Cross-species expression of OsDJ-1C from rice enhances tolerance to salinity and drought stress in tomato
(Elsevier B.V., 2026) Mishra, Manjari; Chatterjee, Yajnaseni; Gupta, Brijesh Kumar; Tomar, Surabhi; Babuta, Priyanka; Gupta, Kapuganti Jagadis; Pareek, Ashwani; Singla-Pareek, Sneh Lata
Abiotic stresses such as salinity and drought induce the accumulation of methylglyoxal (MG), a highly cytotoxic dicarbonyl compound that disrupts cellular metabolism in plants. MG detoxification is primarily mediated by the glutathione-dependent glyoxalase pathway, classically comprising the enzymes glyoxalase I and II. In contrast, glyoxalase III (GLYIII) catalyzes detoxification of MG in a single-step without requiring glutathione. In the present study, we investigated the functional role of OsDJ-1C, a rice GLYIII enzyme, by heterologous overexpression in tomato (Solanum lycopersicum). Transgenic lines exhibited significantly enhanced stress tolerance through a more efficient antioxidant defense mechanism under stress conditions. This improvement was driven by increased GLYIII-mediated detoxification of MG, leading to effective suppression of reactive oxygen species (ROS) accumulation. Reduced ROS levels in the overexpression lines resulted in greater internal oxygen availability and enhanced cellular respiration than wild-type plants. Furthermore, transgenic plants maintained higher pyruvate levels than the wild-type controls, thereby sustaining tricarboxylic acid (TCA) cycle flux and ATP production under stress. Overall, these findings reveal a conserved, cross-species function of OsDJ-1C in enhancing abiotic stress tolerance emphasizing its relevance for improving agricultural sustainability and food security under changing climatic conditions.
Lactate dehydrogenase superfamily in rice and Arabidopsis: Understanding the molecular evolution and structural diversity
(MDPI AG, 2023) Chatterjee, Yajnaseni; Bhowal, Bidisha; Gupta, Kapuganti Jagadis; Pareek, Ashwani; Singla-Pareek, Sneh Lata
Lactate/malate dehydrogenases (Ldh/Maldh) are ubiquitous enzymes involved in the central metabolic pathway of plants and animals. The role of malate dehydrogenases in the plant system is very well documented. However, the role of its homolog L-lactate dehydrogenases still remains elusive. Though its occurrence is experimentally proven in a few plant species, not much is known about its role in rice. Therefore, a comprehensive genome-wide in silico investigation was carried out to identify all Ldh genes in model plants, rice and Arabidopsis, which revealed Ldh to be a multigene family encoding multiple proteins. Publicly available data suggest its role in a wide range of abiotic stresses such as anoxia, salinity, heat, submergence, cold and heavy metal stress, as also confirmed by our qRT-PCR analysis, especially in salinity and heavy metal mediated stresses. A detailed protein modelling and docking analysis using Schrodinger Suite reveals the presence of three putatively functional L-lactate dehydrogenases in rice, namely OsLdh3, OsLdh7 and OsLdh9. The analysis also highlights the important role of Ser-219, Gly-220 and His-251 in the active site geometry of OsLdh3, OsLdh7 and OsLdh9, respectively. In fact, these three genes have also been found to be highly upregulated under salinity, hypoxia and heavy metal mediated stresses in rice.
OsLdh3 interacts with OsGAPC3 and OsLos2 to maintain the glycolytic continuum for tolerance to multiple abiotic stresses in rice
(Oxford University Press, 2026) Chatterjee, Yajnaseni; Babuta, Priyanka; Gupta, Kapuganti Jagadis; Pareek, Ashwani; Singla-Pareek, Sneh Lata
Lactate dehydrogenases are oxidoreductases present in almost all living organisms. They catalyze the interconversion of pyruvate and L-lactate with simultaneous oxidation of NADH and reduction of NAD+. Since their function remains largely unexplored in rice, in this study we deciphered the role of the rice lactate dehydrogenase, OsLdh3. OsLdh3 showed optimum enzyme activity at pH 6.6 for the forward reaction (pyruvate to L-lactate) and pH 9 for the reverse reaction (L-lactate to pyruvate). Protein-protein interaction studies revealed that OsLdh3 interacts with the glycolytic enzymes glyceraldehyde 3-phosphate dehydrogenaseC3 (OsGAPC3) and Enolase2 (OsLos2), suggesting its role in regulating glycolytic flux. Further, overexpression of OsLdh3 in rice showed enhanced abiotic stress tolerance by exhibiting elevated NAD+ levels and OsGAPC3 activity, thereby facilitating an improved glycolytic continuum and higher pyruvate accumulation. Consequently, these lines also showed increased mitochondrial respiration and ATP synthesis, and reduced reactive oxygen species (ROS) accumulation. Further, enhanced photosynthetic efficiency and reduced yield penalty of the stress-imposed OsLdh3 overexpression lines underscore its importance in crop productivity under adverse climatic conditions. Thus, our findings show that OsLdh3 enhances stress tolerance in rice by regulating redox homeostasis and respiration, reducing ROS levels, and maintaining energy balance. This makes OsLdh3 a promising candidate gene for developing climate-resilient rice cultivars with reduced yield gap.