Publications of NIPGR Scientists

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Author: search.filters.author.Yadav, GitanjaliSubject: search.filters.subject.gene duplication

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    StAR-related lipid transfer (START) domains across the rice pangenome reveal how ontogeny recapitulated selection pressures during rice domestication
    (Frontiers Media S.A., 2021) Mahtha, Sanjeet Kumar; Purama, Ravi Kiran; Yadav, Gitanjali
    The StAR-related lipid transfer (START) domain containing proteins or START proteins, encoded by a plant amplified family of evolutionary conserved genes, play important roles in lipid binding, transport, signaling, and modulation of transcriptional activity in the plant kingdom, but there is limited information on their evolution, duplication, and associated sub- or neo-functionalization. Here we perform a comprehensive investigation of this family across the rice pangenome, using 10 wild and cultivated varieties. Conservation of START domains across all 10 rice genomes suggests low dispensability and critical functional roles for this family, further supported by chromosomal mapping, duplication and domain structure patterns. Analysis of synteny highlights a preponderance of segmental and dispersed duplication among STARTs, while transcriptomic investigation of the main cultivated variety Oryza sativa var. japonica reveals sub-functionalization amongst genes family members in terms of preferential expression across various developmental stages and anatomical parts, such as flowering. Ka/Ks ratios confirmed strong negative/purifying selection on START family evolution, implying that ontogeny recapitulated selection pressures during rice domestication. Our findings provide evidence for high conservation of START genes across rice varieties in numbers, as well as in their stringent regulation of Ka/Ks ratio, and showed strong functional dependency of plants on START proteins for their growth and reproductive development. We believe that our findings advance the limited knowledge about plant START domain diversity and evolution, and pave the way for more detailed assessment of individual structural classes of START proteins among plants and their domain specific substrate preferences, to complement existing studies in animals and yeast.
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    Two divergent genes encoding L-myo-inositol 1-phosphate synthase1 (CaMIPS1) and 2 (CaMIPS2) are differentially expressed in chickpea
    (Wiley-Blackwell, 2008) Kaur, Harmeet; Shukla, Rakesh Kumar; Yadav, Gitanjali; Chattopadhyay, Debasis; Majee, Manoj
    L-myo-inositol 1-phosphate synthase (MIPS; EC5.5.1.4) catalyses the rate-limiting step in inositol biosynthetic pathway, and is extremely widespread in living organisms including plants. Several plants possess multiple copies of MIPS gene(s) indicating a possibility of differential expression of each gene to perform distinct physiological functions. To explore this, two MIPS genes (CaMIPS1 and CaMIPS2) were isolated from a drought-tolerant plant chickpea. Both genes are extremely divergent in respect to their introns, at the same time retaining 85% identity to their exons and functionally complementing inositol auxotroph Schizosaccharomyces pombe. Expression analysis showed both genes were expressed in all organs except seed, where only CaMIPS2 transcript was detected. Under environmental stresses, only CaMIPS2 was induced whereas CaMIPS1 expression remained same, which could be explained by the divergence of their 5' upstream regulatory sequences. Remarkably, both gene products exhibited similar biochemical characteristics; however, CaMIPS2 retained higher activity than CaMIPS1 at a high temperature and salt concentration. Furthermore, functional expression of CaMIPS2 in S. pombe results better growth response than CaMIPS1 under stress environment. Taken together, our results suggest that CaMIPS1 and CaMIPS2 are differentially expressed in chickpea to play discrete though overlapping roles in plant; however CaMIPS2 is likely to be evolved through gene duplication to function under environmental stresses.