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Dr. Prem S. Kaushal

Assistant Professor
E-mail: prem dot kaushal at rcb dot res dot in

  • PhD 2010, Indian Institute of Science, Bangalore, INDIA
  • Postdoc, Case Western Reserve University, Cleveland, OH, USA
  • Research Affiliate, Wadsworth Center, Albany, NY, USA
  • Staff Scientist, Centre for DNA Fingerprinting and Diagnostics (CDFD), Hyderabad, INDIA

Structural aspects of protein synthesis in pathogenic organisms

My laboratory’s research goal is to unravel the structural basis of the functioning of large macromolecular complexes, and thereby, to identify potential drug targets. Initially, our focus is to understand the structural aspects of protein synthesis in Mycobacterium tuberculosis (MTb) and in Plasmodium falciparum by applying a multidisciplinary approach of structural biology (cryo- electron microscopy, X-ray crystallography), molecular biology, biochemistry and bioinformatics.

Mtb, causative agent of tuberculosis (Tb), has emerged with drug resistant strains towards currently used drugs. Hence, tuberculosis (Tb) remains a major health threat to the human race. The MTb possesses a unique mechanism to establish a latent tuberculosis infection (LTBI), the dormancy state, capable of its long persistence in the host, even in the presence of functional host immune response. An estimated one third of the world’s population has LTBI and goal is to understand what translation strategy mycobacteria adopts in dormancy.

The P. falciparum that causes most lethal form of malaria has three sites of protein synthesis the cytoplasmic ribosome and two organellar ribosomes, of bacterial origin, reside inside the mitochondria and another inside, a non-photosynthetic relict plastid, the apicoplast. The organellar ribosomes are attractive antimalarial drug targets because of their prokaryotic origin. Our aims are to solve the structures of mitochondrial and apicoplast ribosomes and their functional complexes trapped at different states of protein synthesis.

One of the major bottleneck to achieve high resolution in cryo- EM is to get evenly distributions of particle with optimum ice thickness on the cryo- EM grid. We would like to develop methods to address these issues.

  • Li Y, Sharma MR, Koripella RK, Yong Y, Kaushal PS, Lin Q, Wade JT, Gray TA, Derbyshire KM, Agrawal RK, & Ojha AK. Zinc depletion induces ribosome hibernation in mycobacteria. Proceedings of the National Academy of Sciences USA (PNAS) 115:8191-6.

  • Qu G *, Kaushal PS*, Wang J*, Shigematsu H, Piazza CL, Agrawal RK, Belfort M & Wang HW. Structure of group II intron complexed with its transcriptase. (2016) Nature Structure and Molecular Biology (NSMB) 23, 549-57. (*equal contributions). Highlighted as the News and Views in NSMB 23, 507-9 and a follow up review in RNA BIOLOGY 13, 1218-22.

  • . Kaushal PS*, Sharma MR*, Booth TM, Haque E, Tung C, Sanbonmatsu KY, Spremulli LL and Agrawal R K. (2014) Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosome. Proceedings of the National Academy of Sciences USA (PNAS) 111(20), 7284-9 (*equal contributions).

  • Ahmad MF, Kaushal PS, Wan, Q, Wijeratna SR, An X, Huang M & Dealwis CD. (2012) Role of arginine-293 and glutamine-288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase. Journal of Molecular Biology 419, 315-29.

  • Kaushal PS, Singh P, Sharma A, Muniyappa K & Vijayan M. (2010) X-ray and molecular dynamics studies on Mycobacterium leprae single-stranded DNA binding protein and comparison with other eubacterial SSB structures. Acta Crystallographica D66, 1048-58

  • Kaushal PS, Talawar RK, Varshney U & Vijayan M. (2010) Structure of uracil-DNA glycosylase from Mycobacterium tuberculosis. Insights into interactions with ligands. Acta Crystallographica F66, 887-92 (cover illustration).

  • Kaushal PS, Talawar RK, Krishna PD, Varshney U & Vijayan M. (2008). Unique features of the structure and interactions of mycobacterial uracil-DNA glycosylase: structure of a complex of the Mycobacterium tuberculosis enzyme in comparison with those from other sources. Acta Crystallographica D64, 551-560.

  • Kaushal PS, Sankaranarayanan R & Vijayan M. (2008) Water-mediated variability in the structure of relaxed-state haemoglobin. Acta Crystallographica F64, 463-9.

  • Singh P, Talawar RK, Krishna PD, Varshney U & Vijayan M. (2006) Overexpression, purification, crystallization and preliminary X-ray analysis of uracil N-glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor. Acta Crystallographica F62, 1231-4

Reviews

  • Kaushal PS, Sharma MR and Agrawal RK. (2015) The 55S mammalian mitochondrial ribosome and its tRNA-exit region. Biochimie. 114, 119-26.

  • Wijerathna SR, Ahmad MF, Xu H, Fairman JW, Zhang A, Kaushal PS, Wan Q, Kiser J & Dealwis CG. (2011) Targeting the Large Subunit of Human Ribonucleotide Reductase for Cancer Chemotherapy. Pharmaceuticals, 4(10),1328-54

Book chapters

  • Sharma MR, Kaushal PS, Gupta M, Banavali N K, & Agrawal RK. (2013) Insights into structural basis of mammalian mitochondrial translation. In Translation in Mitochondria and Other Organelles, Duchene, A.M. ed. (Springer-Verlag, Berlin/ Heidelberg), pp. 1-28.

  • Kaushal PS, Wan Q, Faber C, & Dealwis C. (2012) Crystal dehydration Technique. In Crystallography: Research, Technology and Applications, Hokkaido, M. and Nagano, E. ed. (Nova Science Publishers, Inc.), pp. 91-104

Dr. Prem Singh Kaushal
Regional Centre for Biotechnology
NCR Biotech Science Cluster
3rd Milestone, Faridabad-Gurgaon Expressway
P.O. Box No. 3, Faridabad - 121 001
Haryana (NCR Delhi), India
E-mail: prem dot kaushal at rcb dot res dot in
Phone: 91 129-2848980 

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