Institutional Publications

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    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.
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    OsDUF2488 acts synergistically with OsPrx1.1, regulates ROS metabolism and promotes dehydration tolerance in rice
    (John Wiley & Sons, 2025) Gayen, Dipak; Kumar, Sunil; Barua, Pragya; Lande, Nilesh Vikram; Karmakar, Subhasis; Dey, Amit K.; Gayali, Saurabh; Maiti, Tushar Kanti; Molla, Kutubuddin Ali; Murumkar, Snehal; Chakraborty, Subhra; Chakraborty, Niranjan
    Stress-mediated regulation of energy metabolism and its relation to plant adaptation remain largely unknown. Mitochondrial redox potential is greatly influenced by stress-induced reactive oxygen species (ROS); therefore, we mapped the dehydration-induced alterations in the mitochondrial proteome of a resilient rice cultivar, Rasi, generating a proteome map representing the largest inventory of dehydration-responsive mitochondrial proteins from any plant species. Quantitative proteomic analysis led to the identification of an array of dehydration-responsive proteins (DRPs), associated with various cellular functions, conceivably impinging on the molecular mechanism of adaptation. One DRP identified in the mitochondrial proteome was yeast cadmium factor 54 (YCF54-like), also known as DUF (domain of unknown function) and hereafter referred to as OsDUF2488. We demonstrated that OsDUF2488 localises to mitochondria and preferentially interacts with peroxiredoxin, OsPrx1.1. Overexpression of OsDUF2488 in rice caused enhanced tolerance to dehydration and oxidative stress, while CRISPR/Cas9 knockout mutants of OsDUF2488 showed hypersensitivity to dehydration. Upon exposure to dehydration, OsDUF2488 could rescue mitochondrial dysfunction, contributing to increased ATP production in OsDUF2488-overexpressing rice. Coexpression of OsDUF2488 and OsPrx1.1 in yeast demonstrated a mutual effect on enhanced ROS catabolism, suggesting a cross-kingdom adaptive response of OsDUF2488. Our findings suggest that OsDUF2488 acts synergistically with OsPrx1.1 to regulate redox homeostasis and promote stress tolerance in rice.