Browsing by Author "Parveen, Shaista"

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Characterization of the nuclear proteome of a dehydration-sensitive cultivar of chickpea and comparative proteomic analysis with a tolerant cultivar
(John Wiley & Sons Ltd, 2013) Subba, Pratigya; Kumar, Rajiv; Gayali, Saurabh; Shekhar, Shubhendu; Parveen, Shaista; Pandey, Aarti; Datta, Asis; Chakraborty, Subhra; Chakraborty, Niranjan
Water deficit or dehydration hampers plant growth and development, and shrinks harvest size of major crop species worldwide. Therefore, a better understanding of dehydration response is the key to decipher the regulatory mechanism of better adaptation. In recent years, nuclear proteomics has become an attractive area of research, particularly to study the role of nucleus in stress response. In this study, a proteome of dehydration-sensitive chickpea cultivar (ICCV-2) was generated from nuclei-enriched fractions. The LC-MS/MS analysis led to the identification of 75 differentially expressed proteins presumably associated with different metabolic and regulatory pathways. Nuclear localisation of three candidate proteins was validated by transient expression assay. The ICCV-2 proteome was then compared with that of JG-62, a tolerant cultivar. The differential proteomics and in silico analysis revealed cultivar-specific differential expression of many proteins involved in various cellular functions. The differential tolerance could be attributed to altered expression of many structural proteins and the proteins involved in stress adaptation, notably the ROS catabolising enzymes. Further, a comprehensive comparison on the abiotic stress-responsive nuclear proteome was performed using the datasets published thus far. These findings might expedite the functional determination of the dehydration-responsive proteins and their prioritisation as potential molecular targets for better adaptation.
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.
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.
Transcriptional regulation of chickpea ferritin CaFer1 influences its role in iron homeostasis and stress response
(Elsevier B.V., 2018) Parveen, Shaista; Pandey, Aarti; Jameel, Neha; Chakraborty, Niranjan; Chakraborty, Subhra
Ferritin, ubiquitous among all living organisms except yeast, exhibits iron-regulated expression. In plants, this regulation is applied through transcriptional control. Previous studies established the presence of two types of cis-acting elements in the promoter region: the iron regulatory element (FRE) in soybean and the iron-dependent regulatory sequence (IDRS) in maize and Arabidopsis. Adverse environmental conditions (e.g. water-deficit and oxidative stress) are known to modulate the expression of phytoferritin genes. In this study, we cloned and investigated the promoter sequence of a chickpea ferritin, designated CaFer1. Phylogenetic analysis of the CaFer1 promoter revealed its evolutionary relationship with other phytoferritins. The CaFer1 promoter exhibited several putative regulatory elements including two known transcription factor (TF) binding sites, Athb-1 and Myb.Ph. Electrophoretic mobility shift assay confirmed the sequence-specific binding of Athb-1 and Myb.Ph on the CaFer1 promoter. The TF-binding dynamics of CaFer1 showed high induction under conditions of iron-deficiency and water-deficit. We also demonstrated the possible interaction of CaFer1 with IRT1, a key component of the iron uptake system in plants, indicating its involvement in maintaining cellular iron levels. These results provide new insights into the underlying mechanisms of function of these interacting factors in CaFer1-mediated iron homeostasis and the stress response in plants.