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Browsing by Author "Dass, Suchismita"

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    Chickpea ferritin CaFer1 participates in oxidative stress response, and promotes growth and development
    (Nature Publishing Group, 2016) Parveen, Shaista; Gupta, Deepti Bhushan; Dass, Suchismita; Kumar, Amit; Pandey, Aarti; Chakraborty, Subhra; Chakraborty, Niranjan
    Ferritins store and sequester iron, and regulate iron homeostasis. The cDNA for a stress-responsive phytoferritin, previously identified in the extracellular matrix (ECM) of chickpea (Cicer arietinum), was cloned and designated CaFer1. The CaFer1 transcript was strongly induced in chickpea exposed to dehydration, hypersalinity and ABA treatment. Additionally, it has role in the defense against Fusarium oxysporum infection. Functional complementation of the yeast frataxin-deficient mutant, Δyfh1, indicates that CaFer1 functions in oxidative stress. The presence of CaFer1 in the extracellular space besides chloroplast establishes its inimitable nature from that of other phytoferritins. Furthermore, CaFer1 expression in response to iron suggests its differential mechanism of accumulation at two different iron conditions. CaFer1-overexpressing transgenic plants conferred improved growth and development, accompanied by altered expression of iron-responsive genes. Together, these results suggest that the phytoferritin, CaFer1, might play a key role in maintenance of iron buffering and adaptation to environmental challenges.
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    OsAlba1, a dehydration-responsive nuclear protein of rice (Oryza sativa L. ssp. indica), participates in stress adaptation
    (Elsevier B.V., 2014) Verma, Jitendra Kumar; Gayali, Saurabh; Dass, Suchismita; Kumar, Amit; Parveen, Shaista; Chakraborty, Subhra; Chakraborty, Niranjan
    Alba proteins have exhibited great functional plasticity through the course of evolution and constitute a superfamily that spans across three domains of life. Earlier, we had developed the dehydration-responsive nuclear proteome of an indica rice cultivar, screening of which led to the identification of an Alba protein. Here we describe, for the first time, the complete sequence of the candidate gene OsAlba1, its genomic organization, and possible function/s in plant. Phylogenetic analysis showed its close proximity to other monocots as compared to dicot Alba proteins. Protein-DNA interaction prediction indicates a DNA-binding property for OsAlba1. Confocal microscopy showed the localization of OsAlba1-GFP fusion protein to the nucleus, and also sparsely to the cytoplasm. Water-deficit conditions triggered OsAlba1 expression suggesting its function in dehydration stress, possibly through an ABA-dependent pathway. Functional complementation of the yeast mutant ΔPop6 established that OsAlba1 also functions in oxidative stress tolerance. The preferential expression of OsAlba1 in the flag leaves implies its role in grain filling. Our findings suggest that the Alba components such as OsAlba1, especially from a plant where there is no evidence for a major chromosomal role, might play important function in stress adaptation.

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