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 | Dr. Manoj Majee Staff Scientist II PhD: Bose Institute/Jadavpur University, INDIA Postdoctoral Fellow: University of Kentucky, Lexington, USA Email: manoj_majee@nipgr.res.in, majeem@yahoo.co.uk Telephone: 91-11-26735193, Fax: 91-11-26741658 |
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Research Area: |
| Plant Molecular Biology, Biochemistry and Plant Biotechnology. |
Research Programs: |
| Molecular, Genetic and Biochemical study of PROTEIN L- ISOASPARTYL METHYLTRANSFERASE (PIMT) in Plants |
Like other organisms, plants, particularly seeds, suffer spontaneous damage to their proteins due to ageing or environmental stresses. One among several processes that damage proteins is the formation of abnormal isoaspartyl residues.
The accumulation of such spontaneously damaged proteins in a seed or in a plant may be detrimental to its development. Thus the recognition and repair of such altered proteins may be important in limiting protein deterioration in plant cells. One enzyme that appears to participate in this process is the PROTEIN L- ISOASPARTYL METHYLTRANSFERASE (PIMT). PIMT is an ancient enzyme and distributed throughout the phylogenetic domains including plants, but the enzyme has less been thoroughly studied in plants. Functions of this enzyme in plants are not well elucidated.
Our interest is to understand the molecular regulation and functional significance of PIMT gene(s) / proteins in plants and its exploitation to enhance seed vigor, viability, longevity and plant stress adaptation through genetic manipulations. Our research is also directed towards the identification of PIMT substrates/age damaged proteins particularly in seed. |
| Inositol Metabolisms in Plant: A Genomics perspective |
Inositol is essential for the survival of plants in normal as well as environmental stress conditions. It is not only required for to maintain plant growth and development but it also protects cells from the effects of osmotic imbalance caused by environmental stresses. This inositol is produced through the conversion of glucose 6- phosphate to myo inositol 1- phosphate by the enzyme L- myo inositol 1- phosphate synthase (MIPS) and subsequently myo inositol 1 - phosphatase (IMP) produces free inositol.
MIPS coding sequence has been cloned and characterized from a number of widely different organisms including plants. In some plants multiple MIPS/IMP coding genes have been reported; however the significance of these multiple inositol biosynthetic genes in plants has not well been studied. Our interest is to study the significance of inositol biosynthetic gene families in plants through molecular characterization of each gene member and their functional characterization through mutant analysis. Our laboratory is also focused on the biosynthesis and metabolism of inositol and its derivatives and how these processes impact on physiology of plants particularly under environmental stresses. |
| Molecular Genetic and Biochemical Study of Ubiquitin /26S Proteasome Pathway in Seed Physiology and Plant Stress Adaptation |
Plant growth, development and environmental adaptations are mostly controlled by the selective removal of short lived regulatory proteins. One major proteolytic pathway to remove these regulatory proteins in eukaryotes is the ubiquitin (Ub)/ 26S proteasome pathway. In plants, this pathway plays a crucial role in the control of many different cellular processes like embryogenesis, hormonal regulations, flowering, senescence, photo morphogenesis, circadian rhythm, pathogen resistance and environmental adaptation. The genome of Arabidopsis encodes more than 1400 (>5% of the proteome) pathway components which is more than twice that of yeast, Drosophila, mice and human. Why plants have placed a particular emphasis on this proteolytic system is poorly understood. How E3s are regulated and what are the substrates of the Ub/26S proteasome pathway in plants are big queries for the plant biology research.
Our laboratory is attempting to elucidate the role of this proteolytic pathway in seed biology and plant stress adaptation. What specific function does this pathway in seed biology and environmental adaptation and how this pathway be constructively manipulated? |
Selected Publications: |
 | Verma P, Singh A, Kaur H and Majee M (2010) PROTEIN L- ISOASPARTYL METHYLTRANSFERASE1 (CaPIMT1) from chickpea mitigates oxidative stress induced growth inhibition of Escherichia coli. Planta 231: 329-336. |
 | Kaur H, Shukla RK, Yadav G, Chattopadhyay D and Majee M (2008) Two divergent genes encoding L-myo-inositol 1 -phosphate synthase1 (CaMIPS1) and 2 (CaMIPS2) are differentially expressed in chickpea. Plant, Cell and Environment 31: 1701-1716. |
 | Shen H, Zhu L, Castillon L, Majee M, Downie B and Huq E (2008) Light-induced phosphorylation and degradation of the negative regulator PIF1 depends upon its direct physical interactions with photoactivated phytochromes. The Plant Cell 20: 1586-1602. |
 | Salatia L, Kar RK, Majee M and Downie B (2005) Identification and characterization of mutants capable of rapid seed germination at 10oC from activation tagged lines of Arabidopsis thaliana. Journal of Experimental Botany 56: 2059-2069. |
 | Majee M, Patra B , Mundree S and Majumder AL (2005) Molecular cloning, bacterial expression and characterization of L-myo-inositol 1-phosphate synthase from a monocotyledonous resurrection plant Xerophyta Viscosa Baker. Journal of Plant Biochemistry and Biotechnology 14: 95-99. |
 | Majee M, Maitra S, Dastidar KG, Pattanaik S, Chatterjee A, Hait N, Das KP and Majumder AL (2004) A novel salt-tolerant L-myo-inositol 1- phosphate synthase from Porteresia coarctata Tateoka, a halophytic wild rice: Molecular cloning, bacterial overexpression, characterization and functional introgression into tobacco conferring salt-tolerance phenotype. Journal of Biological Chemistry 279: 28539-28552. |
 | Chatterjee A, Majee M, Ghosh S and Majumder AL (2004) sll1722, an unassigned ORF of Synechocystis PCC 6803, codes for L-myo-Inositol 1-phosphate synthase. Planta 218: 989-998. |
 | Bhattacharya J, Dastidar KG, Chatterjee A, Majee M, Majumder AL (2004) Synechocystis Fe superoxide dismutase gene confers oxidative stress tolerance to Escherichia coli. Biochemical and Biophysical Research Communication 316: 540-544. |
 | Majumder AL, Chatterjee A, Dastidar KG and Majee M (2003) Diversification and evolution of L -myo inositol 1- phosphate synthase. FEBS Letters 553: 3-10. |
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Book Chapter: |
 | Majumder AL, Hait NC, Deb I, Majee M, Chatterjee A, Dastidar KG, Bhattacharyya S, Ghosh S, Chatterjee A, Maitra S and Pattanaik S (2003) L-myo Inositol 1-Phosphate Synthase: an ancient protein with diverse function. In Molecular Insight in Plant Biology. P. Nath, A.K. Mattoo, S.A. Ranade and J.H. Weil (Editors), Publishers: Oxford & IBH Publishing Co.Pvt. Ltd; New Delhi, India. Chapter 5, pp67- 76. |
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Patent: |
 | Patent application # PAT/4.1.4/02019/2003 dated March 17th, 2003. United States Patent 20060148059 Kind Code: A1 "A salt Tolerant L-myo-Inositol 1 Phosphate Synthase and a process of obtaining the same". (Inventors: A. Lahiri Majumder and M. Majee). |
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Group Members: |
 | Ms. Harmeet Kaur | Ph.D. Student |
 | Ms. Pooja Verma | Ph.D. Student |
 | Mr. Bhanu Prakash Petla | Ph.D. Student |
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