National Institute of Plant Genome Research
 
    Dr. Manoj Majee
    Staff Scientist IV
    PhD: Bose Institute/Jadavpur University, INDIA
    Postdoctoral Fellow: University of Kentucky, Lexington, USA
    Email: manojmajee@nipgr.ac.in, majeem@yahoo.co.uk
    Telephone: 91-11-26735193, Fax: 91-11-26741658
 Honors/Awards :
Medal for Young Scientist  (2011) from the Indian National Science Academy (INSA).
Young Scientist Platinum Jubilee Award (2011) from the National Academy of Sciences (NASI), India.
 Research Area:
Seed Biology and Plant Stress Adaptation/Plant Molecular Biology and Biochemistry.
 Group Members:
 Research Programs:
Our lab primarily investigates the regulation and role of protein repairing enzymes, inositol metabolism and ubiquitin /26S proteasome pathway in seed biology and plant stress adaptation.
PROTEIN L- ISOASPARTYL METHYLTRANSFERASE (PIMT)
Proteins and peptides are the most significant macromolecules which carry out the essential functions of the cell. They are susceptible to a variety of spontaneous modifications as they age and also in stressful conditions. Among such protein modifications, conversion of L-aspartyl or asparaginyl residues to abnormal isoaspartyl (isoAsp) residues in proteins is quite prevalent among organisms. However, this damage could be repaired by the protein repairing enzyme PROTEIN L-ISOASPARTYL METHYLTRANSFERASE (PIMT). PIMT is a widely distributed protein repairing enzyme which catalyzes the conversion of abnormal L-isoaspartyl residues in spontaneously damaged proteins to normal aspartyl residues. This enzyme is encoded by two divergent genes (PIMT1 & PIMT2) in plants in contrast to bacterial or animal systems, where such enzymes are encoded by a single gene. The role of PIMT is not well elucidated in higher plants. Based on the occurrence of high PIMT activity in quiescent and germinating seeds, the role of PIMT in seed vigor and longevity has been suggested.

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, and 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 Metabolism
Inositol has been shown to be an essential component for plant growth and development; therefore plants maintain inositol pool at basal level throughout their life cycle. However, not all but few stress tolerant plants like ice plant or chickpea were shown to elevate their inositol level in response to environmental stresses, possibly to meet additional demand of inositol which might be required for their adaptation to 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.

Our interest is to study the environmental regulation of inositol biosynthetic pathway, through molecular and functional analysis of each inositol biosynthetic gene.
Ubiquitin /26S Proteasome Pathway
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?
 Complete list of Publications & Patents
As a Corresponding Author & PI at NIPGR
Saxena SC, Salvi P, Kaur H, Verma P, Petla BP, Rao V, Kamble N  and Majee M (2013) Differentially expressed myo-inositol monophosphatase gene (CaIMP) in chickpea (Cicer arietinum L.) encodes a lithium sensitive phosphatase enzyme with broad substrate specificity and improves seed germination and seedling growth under abiotic stresses Journal of Experimental  Botany (in press).
Verma P, Kaur H,  Petla BP, Rao V, Saxena SC and Majee M (2013) PROTEIN L- ISOASPARTYL METHYLTRANSFERASE2 gene is differentially expressed in chickpea and enhances seed vigor and longevity by reducing abnormal isoaspartyl accumulation predominantly in seed nuclear proteins. Plant Physiology 161:1141-1157.
Kaur H, Verma P,  Petla BP, Rao V, Saxena SC and Majee M (2013) Ectopic expression of the ABA inducible dehydration responsive chickpea L-myo-inositol 1 -phosphate synthase 2 (CaMIPS2) in Arabidopsis enhances tolerance to salinity and dehydration stress. Planta 237: 321-335.
Verma P and Majee M (2013) Seed Germination and Viability Test in Tetrazolium (TZ) Assay. bio-protocol .org (invited)
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.
 
Patent filed
Patent filed # 23/DEL/2012 (January 4th 2012) “SEED VIGOR ASSOCIATED POLYNUCLEOTIDE SEQUENCES   FROM CHICKPEA AND USES THEREOF” (Inventor: Manoj Majee & Pooja Verma, NIPGR, New Delhi, India).
 
Book Chapters
Saxena S C, Kaur H, Verma P, Petla B P, Rao V,  Majee M (2012) Osmoprotectants: Potential for Crop Improvement under Adverse Conditions. In Plant Acclimation to Environmental Stress, ed by Tuteja & Gill. Springer Science + Business Media, LLC 233 Spring Street, New York, NY 10013, USA.
Majee M and Kaur H (2011) L- myo-inositol 1-phosphate synthase (MIPS) in chickpea: gene duplication and functional divergence. In Gene Duplication ed. by Felix Fredburg: Intech (ISBN 978-953-307-387-3).
 
As a CoPI /Collaborator at NIPGR
Garg R, Verma M, Agrawal S, Shankar R, Majee M and Jain M (2013) Deep transcriptome sequencing of wild halophyte rice, Porteresia coarctata, provides novel insights into the salinity and submergence tolerance Factors. DNA Research (in press).
Augustine R, Majee  M,   Gershenzon J and     Bisht  N (2013)  Four genes encoding MYB28, a major transcriptional regulator of aliphatic glucosinolate pathway, are differentially expressed in allopolyploid Brassica juncea. Journal of Experimental  Botany (in press).
Bhatt D, Saxena SC, Jain S, Dobriyal A K, Majee M  and Arora S (2013) Cloning, expression and functional validation of drought inducible ascorbate peroxidase (Ec-apx1) from Eleusine coracana. Molecular Biology Reports 40:1155-1165.
Lata C, Bhutty S, Bahadur RP, Majee M and Manoj Prasad (2011) Association of SNP in a novel DREB2-like gene SiDREB2 with stress tolerance in foxtail millet (Setaria italica L.). Journal of Experimental Botany 62: 4731-4748.
 
As a Post Doc Fellow at University of Kentucky, USA
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.
 
As a PhD student at Bose Institute, Kolkata
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.
 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.
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, Bose Institute, Kolkata, India