National Institute of Plant Genome Research
 
    Prof. Asis Datta
    (Ph.D., D.SC., FNA., FASc., FTWAS)
    Professor of Eminence
 Career
Government of India Fellow Bose Institute, Calcutta. (1964-1968)
Research Associate, Public Health Research Institute New York, USA (1968-1971)
Assistant Virologist, University of California Los Angeles, USA (1971-1973)
Visiting Scientist, Roche Institute of Molecular Biology, NY USA (1976-1977, 1980-1981)
Associate Professor, School of Life Sciences, JNU (1975-1978)
Professor, School of Life Sciences, JNU (1978-2002)
Dean & Professor, School of Life Sciences, JNU (1983-1985)
Rector & Professor, JNU (1993-1996)
Vice-Chancellor, JNU. As Vice-Chancellor, created several new schools and centres. (1996-2002)
Founder Director, National Institute of Plant Genome Research. (2002-2008)
Professor of Eminence, NIPGR. (2009-present)
 Awards and Honors
Awarded Shanti Swaroop Bhatnagar Prize in Biological Sciences by CSIR (1980); Fellow, Indian National Sciences Academy, New Delhi; Fellow, Indian Academy of Sciences, Bangalore; Fellow, National Science Academy, Allahabad; Fellow, Third World Academy of Sciences, Italy; Guha Memorial Award (1988); Sir Amulya Rattan Oration Award (1988); First GD Birla Award for Science and Technology (1991); Dr. Nitya Anand Endowment Award, INSA (1993); The Federation of Indian Chamber of Commerce and Industry Award for R&D in Life Sciences (1994); Om Bhasin Award for Science and Technology (1995); Third World Academy of Sciences Awards (TWAS) for Biology (1996); Goyal Prize in Life Sciences (1996);  Ranbaxy Award in Medical Sciences (Basic Research) for the year 1996; D.M Bose Gold Medal, Indian Science News Association (1996); Government of India honored Professor Asis Datta with Padma Shree (1999); General President, Society of Biological Chemistry (2000); Indira Gandhi Priyadarshini Award (2000); R.D Birla Award for Biochemistry and Molecular Biology (2001);  Dr. B. R. Ambedkar Centenary Award for Excellence in Biomedical Research, ICMR, Govt. of India (2003); General President of Indian Science Congress Association for 2003-2004; Bashambar Nath Chopra Lecture Award (2004); Life Time Achievement, Society of Biological Chemists (2005); P.C. Mahalanabish Memorial award, West Bengal, Science & Technology (2005); Sir Edward Melbary Oration award (2006); Degree of Doctor of Science (Honoris Causa) in 2002, 2004 and 2008 awarded by The University of Burdwan, Bidhan Chandra Agricultural University and Vidyasagar University, respectively for wide ranging contributions. Recognized Emeritus Professor of Jawaharlal Nehru University. Asutosh Mookerjee Medal Award at the 92nd Session of Indian Science Congress (2005); Life time achievement award, Indian Science Congress (2006). Awarded Padma Bhushan by Government of India (2008).
 Current Research Programme
A. Molecular Biology of Pathogenic Yeast Candida albicans.
We are working in the area of molecular biology of pathogenic yeast using Candida albicans as a model system with an aim to understand the nature of virulent factors associated with the medically important yeast. Candida albicans, is the most pathogenic of Candida species. It is a serious agent of infection particularly in immuno compromised patients. The delicate balance between the host and the otherwise normally commensally fungus, turn into a parasitic relationship, resulting in the development of infection is called candidiasis. It is believed that for C. albicans to become invasive, a change from yeast to hypha is important. Yeast to hypha conversion occurs through an intermediate germ tube stage. The germ tube leads to hyphae formation. N-acetylglucosamine (GlcNAc) is utilized by the pathogenic strains of C. albicans. GlcNAc also induces change in cellular morphology in C. albicans. Morphogenetic changes like hyphae and pseudohyphal growth enables to propagate into the host tissue as a preliminary manifestation of invasion and spread of pathogens. To elucidate the role of GlcNAc in pathogen city, NAG1 has been cloned in our laboratory. GlcNAc transcriptionally induces NAG1. Sequence analysis of a 4 kb genomic clone containing NAG1 indicates that this gene is part of a cluster containing two other genes of the GlcNAc catabolic pathway: DAC1 (GlcNAc-6- phosphate deacetylase) and HXK1 (GlcNAc kinase). Clusters of functionally related genes are general features of prokaryotes and are less prevalent in eukaryotes. In E. coli the amino sugar pathway genes are also organized in clusters and possibly have a common regulatory mechanism. This is the first report of a gene cluster in Candida [M. Jyothi Kumar, Md. S. Jamaluddin, K. Natarajan, Deepinder Kaur and Asis Datta. Proc. Natl. Acad. Sci, USA 97: 14218-14223, 2000]. Interestingly, attenuation of virulence occurs by disruption of this pathway [Praveen Singh, Sharmistha Ghosh and Asis Datta), Infection and Immunity, 69 (12), 7898-7903 (2001).
B. Crop Improvement Program.
Collaborators : Dr. Niranjan Chakraborty and Dr. Subhra Chakraborty (as a part of nutritional genomics group).
I. Nutritional improvement of crop plants by expressing a seed albumin gene from Amaranthus hypochondriacus.
In our laboratory, we have been working on crop improvement program for last couple of years. In order to develop transgenic crop plants with high nutritional value, a seed albumin gene (AmA1) encoding for a protein of high lysine and sulfur containing amino acids from amaranth seeds has been cloned and sequenced. [Raina A and Datta A. Proc. Natl. Acad. Sci. USA 89:11774-11778, 1992]. Very recently, the AmA1 gene has been introduced into potato plants. The expression of AmA1 in transgenic plants, both constitutively and tuber-specifically, resulted in a significant increase in growth and tuber yield besides an increase in most essential amino acids. The transgenic tubers also contained more total protein as compared to control potato tubers [Chakraborty, S., Chakraborty, N and Datta, A. Proc. Natl. Acad. Sci. USA 97: 3724-3729, 2000]. Field trial of India's first GM crop (GM potato) with high nutritional value is now over in collaboration with the Central Potato Research Institute (CPRI). In addition, the technology in the industrial processing of animal feed supplement using yeast cells expressing AmA1 protein, has been transferred to Cadila Pharmaceuticals for commercial production.
II. Expression of oxalate decarboxylase reduces the accumulation of oxalic acid in crop plants and confers fungal resistance.
Some green leafy vegetables (e.g. amaranth, spinach, rhubarb) are rich sources of vitamins and minerals but they contain oxalic acid as a nutritional stress factor because oxalate chelates calcium and precipitation of calcium oxalate in kidney leads to hyperoxaluria and destruction of renal tissues. In addition, the production of oxalic acid is an important attacking mechanism utilized by several phytopathogenic fungi, e.g. Sclerotinia sclerotiorum, Sclerotinia rolfsii, and Sclerotinia ceptivorum. In order to develop transgenic plants with low oxalic content and making them resistant to fungal infection, a DNA (OXDC) encoding oxalate decarboxylase from Collybia velutipes has been isolated and sequenced [Mehta, A and Datta, A. J. Biol. Chem. 266:23548-23553, 1991].
Very recently, oxalate-free transgenic tobacco and tomato plants have been developed which are resistant to phytopathogenic fungus Sclerotinia sclerotiorum [Keswarni, M., Azam, M., Natarajan, N., Mehta, A and Datta, A. J. Biol. Chem. 275:7230-7238, 2000]. Oxalate- free GM tomatoes resistant to pathogenic fungus are currently under field trial.
III. Enhanced self life in fruit by using novel genes which are involved in fruit ripening.
C. Functional Genomics
Collaborators : Dr. Niranjan Chakraborty and Dr. Subhra Chakraborty.
I. Differential gene expression in chick-pea - Fusarium interaction.
II. Isolation of genes from drought - responsive proteome of legumes and Cereals.
 Contact
Phone: (0): 91-11- 26742750; 26741612,14,17 Ext.-119;
Direct: 26735119
(L): 26741612,14,17 Ext. - 179; Direct: 26735179
(R): 26174237; 26741612,14,17 Ext.- 123, 126
FAX: 91-11-26741658
E-mail: asisdatta@hotmail.com, asis_datta@nipgr.res.in & asis_datta@rediffmail.com
 Selected Publications
Biswas S, Van DP and Datta A (2007) Environmental sensing and signal transduction pathways regulating morphopathogenic determinants of Candida albicans. Microbiol Mol Biol Rev. 71(2): 348-76.
Chakraborty S, Chakraborty N, Jain D, Salunke DM and Datta A (2002) Active site geometry of oxalate decarboxylase from Flammulina velutipes: Role of histidine coordinated manganese in substrate recognition. Protein Sci. 11(9): 2138-47.
Chakaraborty S, Sarma B, Chakraborty N and Datta A (2002) Premature termination of RNA polymerase II mediated transcription of a seed protein gene in Schizosaccharmyces pombe. Nucleic Acid Research. 30: 1940-2949.
Singh P, Ghosh S and Datta A (2001) Attenuation of virulence and changes in morphology in Candida albicans by disruption of the N-acetylglucosamine catabolic pathway. Infection and Immunity. 69 (12): 7898-7903, 2001.
Kumar MJ, Jamaluddin MS, Natarajan K, Kaur D and Datta A (2000) Analysis of the Inducible GlcNAc Catabolic Pathway Gene Cluster in Candida albicans: Discrete GlcNAc Inducible Factors interact at the Promoter of NAG1. Proc. Natl. Acad. Sci, USA 97: 14218-14223.
Chakraborty S, Chakraborty N and Datta A (2000) Increased nutritive value of transgenic potato by expressing a nonallergenic seed albumin gene from Amaranthus hypochondriacus Proc. Natl. Acad. Sci, USA, 97: 3724-3729.
Kesarwani M, Azam M, Natarajan K, Mehta A and Datta A (2000) Oxalate Decarboxylase from Collybia velutips: Molecular Cloning and Its Over Expression to Confer Resistance to Fungal Infection in Transgenic Tobacco and Tomato. J. Biol. Chem. 275: 7230-7238.
Malathi K, Ganesan K and Datta A (1994) Identification of a putative transcription factor in Candida albicans that can complement the mating defect of Saccharomyces cerevisiae ste12 mutants. J. Biol. Chem. 269: 22945- 22951.
Natarajan K and Datta A (1993) Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-phosphate deaminase from Candida albicans. J. Bio. Chem. 268: 9206-9214.
Raina A and Datta A (1992). Molecular cloning of a gene encoding a seed specific protein with nutritionally balanced amino acid composition from Amaranthus. Proc. Natl. Acad. Sci. USA. 89: 11774-11778.
Mehta A and Datta A (1991) Purification, characterization and cDNA cloning of inducible oxalate decarboxylase from Collybia velutipes. J. Biol. Chem. 266: 23548-23553.
Ganesan K, Banerjee A and Datta A (1991) Molecular Cloning of Secretary acid proteinase gene from Candida albicans and its use as a species specific probe. Infection and Immunity 59: 2972-2977.
Toro N, Datta A, Yanofsky M and Nester EW (1988) Role of the Overdrive Sequence in T-DNA border cleavage in Agrobacterium. Proc. Natl. Acad. Sci. USA. 85: 8558-8562.
Reddy ASN, Raina A, Gunnery S and Datta A (1987) Regulation of protein synthesis in plant embryo by protein phosphorylation. I. Purification and characterization of a cAMP-independent protein kinase and its endogenous substrate. Plant Physiol. USA, 83: 988-993.
Singh B, Biswas M and Datta A (1980) Inducible N-acetylglucosamine binding protein in yeasts. J. Bacteriol. 144: 1-6.
Singh B and Datta A (1979) Induction of N-acetylglucosamine catabolic pathway in spheroplasts of Candida albicans Biochem. J. 178: 427-431.
Datta A, De Haro C, Sierra JM and Ochoa S (1977) Mechanism of translational control by hemin in reticulocyte lysate. Proc. Natl. Acad. Sci. USA. 74: 3326-3329.
Datta A and Franklin RM (1972) DNA-dependent RNA polymerase is associated with bacteriophage PM2. Nature 236 131-133.
Datta A, Camerini-Otero RD, Braunstein SN and Franklin RM (1971) Structure and synthesis of a lipid containing bacteriophage VII. Structural proteins of bacteriophage PM2. Virology 45: 232-239.
Datta A (1970) Regulatory role of ATP on hog kidney N-acetyl-D-glucosamine-2-epimerase. Biochemistry 9: 3363-3370.
 Patents
A process for the preparation of DNA encoding Oxalate decarboxylase from Collybia velutipes Indian Patent No. 425/Del/92 dated 18.5.92.
A process for the isolation of DNA encoding a seed specific protein with nutritionally balanced amino acid composition from Amaranthus Indian Patent No. 227/Del/93 dated 10.03.93.
Oxalate decarboxylase US Patent No 5547870 issued on 20.8.96
Seed storage protein with nutritionally balanced amino acid composition US Patent No.5670635 issued on 23.9.97
AmA1 protein and presumably a composition containing same US Patent No.5849352 issued on 15. 12. 98
Method of making seed specific DNA US Patent No.5846736 issued on 8.12.98