Publications of NIPGR Scientists

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Author: search.filters.author.Hazra, AbhijitSubject: search.filters.subject.Chickpea

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    Identification, genomic organization, and comprehensive expression analysis reveals the implication of Cicer arietinum SKP1-like genes in abiotic stress
    (Springer Nature Publishing AG, 2023) Varshney, Vishal; Hazra, Abhijit; Majee, Manoj
    Ubiquitin-mediated proteolysis is a central pathway that controls protein turnover. Ubiquitin–proteasome pathway works sequentially to ubiquitinate appropriate substrates that subsequently lead to its degradation via 26S proteasome. Among the several classes of ubiquitin E3 ligases, the SKP1-Cullin-F-box class is generally the most common and widely explored. SKP1-like proteins in plants have gained less attention than other SCF complex components, although they have a larger involvement in controlling wide aspects of vascular plants. Several studies have shown that SKP1-like proteins regulate abiotic stress tolerance on their own, in addition to working in the SCF complex. However, the identification and characterization of SKP1-like genes in chickpea are missing. In the present study, we have identified 15 SKP1-like genes in the chickpea genome that have been categorized into three types type Ia, type Ib, and type II based on the structure and sequence. The evolutionary conservation of the chickpea SKP1 family with dicots and monocots was discovered utilizing phylogenetic analysis. The presence of hormone, plant growth and development, and various stress-related cis-regulatory elements in all chickpea SKP1-like gene promoters showed that SKP1-like genes have a potential role in functions in hormone and various abiotic stress signaling in chickpea. According to the qRT-PCR expression study, most chickpea SKP1-like genes are differently expressed under three abiotic stresses; namely drought, salt, and oxidative stress. As a result, the current work offers up new possibilities for leveraging SKP1-related data to better understand the role of abiotic stress tolerance in the chickpea plant.
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    A conserved NAG motif is critical to the catalytic activity of galactinol synthase, a key regulatory enzyme of RFO biosynthesis
    (Portland Press, 2021) Salvi, Prafull; Kumar, Bhavnesh; Kamble, Nitin Uttam; Hazra, Abhijit; Majee, Manoj
    Galactinol synthase (GolS) catalyzes the key regulatory step in the biosynthesis of Raffinose Family Oligosaccharides (RFOs). Even though the physiological role and regulation of this enzyme has been well studied, little is known about active site amino acids and the structure-function relationship with substrates of this enzyme. In the present study, we investigate the active site amino acid and structure function relationship for this enzyme. Using a combination of three-dimensional homology modelling, molecular docking along with a series of deletion, site directed mutagenesis followed by in vitro biochemical and in vivo functional analysis; we have studied active site amino acids and their interaction with the substrate of chickpea and Arabidopsis GolS enzyme. Our study reveals that the GolS protein possesses GT8 family-specific several conserved motifs in which NAG motif plays a crucial role in substrate binding and catalytic activity of this enzyme. Deletion of entire NAG motif or deletion or the substitution (with alanine) of any residues of this motif results in complete loss of catalytic activity in in vitro condition. Furthermore, disruption of NAG motif of CaGolS1 enzyme disrupts it’s in vivo cellular function in yeast as well as in planta. Together, our study offers a new insight into the active site amino acids and their substrate interaction for the catalytic activity of GolS enzyme. We demonstrate that NAG motif plays a vital role in substrate binding for the catalytic activity of galactinol synthase that affects overall RFO synthesis.