Publications of NIPGR Scientists

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Author: search.filters.author.Barua, PragyaSubject: search.filters.subject.dehydration tolerance

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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.
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    Dehydration-responsive chickpea chloroplast protein, CaPDZ1, confers dehydration tolerance by improving photosynthesis
    (John Wiley & Sons, 2022) Lande, Nilesh Vikram; Barua, Pragya; Gayen, Dipak; Wardhan, Vijay; Jeevaraj, Theboral; Kumar, Sunil; Chakraborty, Subhra; Chakraborty, Niranjan
    The screening of a dehydration-responsive chloroplast proteome of chickpea led us to identify and investigate the functional importance of an uncharacterized protein, designated CaPDZ1. In all, we identified 14 CaPDZs, and phylogenetic analysis revealed that these belong to photosynthetic eukaryotes. Sequence analyses of CaPDZs indicated that CaPDZ1 is a unique member, which harbours a TPR domain besides a PDZ domain. The global expression analysis showed that CaPDZs are intimately associated with various stresses such as dehydration and oxidative stress along with certain phytohormone responses. The CaPDZ1-overexpressing chickpea seedlings exhibited distinct phenotypic and molecular responses, particularly increased photosystem (PS) efficiency, ETR and qP that validated its participation in PSII complex assembly and/or repair. The investigation of CaPDZ1 interacting proteins through Y2H library screening and co-IP analysis revealed the interacting partners to be PSII associated CP43, CP47, D1, D2 and STN8. These findings supported the earlier hypothesis regarding the role of direct or indirect involvement of PDZ proteins in PS assembly or repair. Moreover, the GUS-promoter analysis demonstrated the preferential expression of CaPDZ1 specifically in photosynthetic tissues. We classified CaPDZ1 as a dehydration-responsive chloroplast intrinsic protein with multi-fold abundance under dehydration stress, which may participate synergistically with other chloroplast proteins in the maintenance of the photosystem.