Jayati Sengupta , Ph.D.

Chief Scientist
Structural Biology & Bioinformatics
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Research Interest

My laboratory is engaged in a research program that combines structural biology with functional studies of cellular macromolecular machines with a particular focus on the protein synthesis machinery of the cell. I was fascinated by the structure and function of the astounding molecular machine ribosome during my post doctoral studies in Prof. Joachim Frank’s ribosome research lab and when I started my own research group at IICB, I have decided to continue research in understanding various ribosome-related pathways in bacteria.

Pathogenic bacteria often face major stresses inside human body. Cells express many ribosome-interacting factors which show regulatory function upon binding to the ribosome under various environmental stresses.  However, the understanding of the molecular mechanisms of many of these regulatory processes has remained unknown, despite their biological importance.

One of the major goals of my lab is to understand functional role of ribosome-associated, stress-related factors in pathogenic organisms primarily using cryo-electron microscopy (cryo-EM) and single particle image analysis technique. In addition, in collaboration with other research laboratories, we also employ cryo-EM for structural characterization of various bio-macromolecular assemblies with the aim of understanding their roles in health and diseases.

Credentials

  • Chief Scientist (2024-till date), CSIR-IICB, Kolkata
  • Senior Principal Scientist (2018-2024), CSIR-IICB, Kolkata
  • Principal Scientist (2012-2018), CSIR-IICB, Kolkata
  • Senior Scientist (2008-2012), CSIR-IICB, Kolkata
  • Research Scientist (2006-April2008), Wadsworth Center, Albany, New York, USA 
  • Research Affiliate (2000-2005), Wadsworth Center, Albany, New York, USA
  • Ph.D. (1997) North Eastern Hill University (NEHU), Shillong, India, in Chemistry

Patents & Publications

  1. Baid, P. and Sengupta, J.* (2025) Cryo-EM structures reveal a unique role of Elongation Factor G2 in mycobacteria. FEBS J. (Accepted)
  2. Banerjee, A, Krishnamoorthi Srinivasan, K., Sengupta, J.* (2025) Mycobacterial methionine aminopeptidase type 1c moonlights as an antiassociation factor on the 30S ribosomal subunit. J. Mol. Biol May 27:169230 (available online).
  3. Banerjee, A., Dey, S, Srinivasan, S., Dhur, A., Baid, P. Sengupta, J.* (2025). Mycobacterium smegmatis Ribosome Purification, Co-sedimentation, and Subunit Association Assay. Bio-protocol 15(10): e5318. 
  4. Krishnamoorthi S, Banerjee A, Sengupta J. (2024) Cryo-EM structures reveal a molecular mechanism underlying HflX-mediated erythromycin resistance in mycobacteria, Structure (Cell Press), Just Accepted
  5. Baid P, Sengupta J. (2023) Cryo-EM captures a unique conformational rearrangement in 23S rRNA helices of the Mycobacterium 50S subunit Int J Biol Macromol., Sep 12;253(Pt 3):126876 (Online)
  6. Mozumder S, Bej A, Sengupta, J. (2022) Ligand-Dependent Modulation of the Dynamics of Intracellular Loops Dictates Functional Selectivity of 5-HT2AR, J Chem Inf Model. (ACS) 62(10), 2522-2537.  (Cover Art selected)
  7. Bhattacharjee, S., Sengupta, J. (2021) Hidden electrostatic energy contributions define dynamic allosteric communications within p53 during molecular recognition. Biophysical J. (Cell Press), 120(20):4512-4524. 
  8. Akbar, S., Bhakta, S., Sengupta, J. (2021) Structural insights into the interplay of protein biogenesis factors with the 70S ribosome. Structure (Cell Press), 29(7), 755-767.
  9. Chakraborty, R., Dey, S., Sil, P., Paul, S.S., Bhattacharyya, D., Bhunia, A., Sengupta, J., Chattopadhyay, K. (2021) Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects Commun Biol. (Nature), 4(1), 518.
  10. Bhattacharjee, S., Bhattacharyya, R., Sengupta, J. (2021) Dynamics and electrostatics define an allosteric druggable site within the receptor-binding domain of SARS- CoV-2 spike protein. FEBS Lett., 595(4), 442-451. [Journal cover as Editor’s choice]
  11. Banerjee, A., Bhakta, S., Sengupta, J. (2021) Integrative approaches in cryogenic electron microscopy: Recent advances in structural biology and future perspectives. iScience, 24(2), 102044. [Invited review]
  12. Ferdosh, S., Banerjee, S., Pathak, B.K., Sengupta, J., Barat, C. (2021) Hibernating ribosomes exhibit chaperoning activity but can resist unfolded protein-mediated subunit dissociation. FEBS J. 288(4):1305-1324.
  13. Sarkar, P., Mozumder, S., Bej, A., Mukherjee, S., Sengupta, J., Chattopadhyay, A. (2020) Structure, dynamics and lipid interactions of serotonin receptors: excitements and challenges. Biophys Rev., 13(1),101–22. [Review]
  14. Bhattacharyya, R., Bhattacharjee, S., Pathak, B.K., Sengupta J.  (2020) Heptameric Peptide Interferes with Amyloid-β Aggregation by Structural Reorganization of the Toxic Oligomers. ACS Omega. 5(26):16128-16138.
  15. Pathak, B.K., Das, D., Bhakta, S., Chakrabarti, P., Sengupta J. (2020) Resveratrol as a nontoxic excipient stabilizes insulin in a bioactive hexameric form. J Comput Aided Mol Des. 34(8):915-927.
  16. Akbar, S., Mozumder, S., Sengupta, J. (2020) Retrospect and Prospect of Single Particle Cryo-Electron Microscopy: The Class of Integral Membrane Proteins as an Example. J Chem Inf Model. 60(5):2448-2457. [Review]
  17. Mozumder, S., Mahesh, G., Srinivasan, K., Sengupta, J., Mukherjee S. (2020) Expression and Purification of Functionally Active Serotonin 5-HT 2A Receptor in Insect Cells Using Low-titer Viral Stock Bio Protoc. 10(15):e3704.
  18. Mozumder, S., Bej, A., Srinivasan, K., Mukherjee, S., Sengupta, J. (2020) Comprehensive structural modeling and preparation of human 5-HT2A G-protein coupled receptor in functionally active form. Biopolymers. 111(1):e23329.
  19. Ghosh, R., Kaypee, S., Shasmal ,M., Kundu, T.K., Roy, S., Sengupta, J. (2019) Tumor Suppressor p53-Mediated Structural Reorganization of the Transcriptional Coactivator p300. Biochemistry (ACS) 58(32):3434-3443.
  20. Bhakta, S., Akbar, S., Sengupta, J. (2019) Cryo-EM Structures Reveal Relocalization of MetAP in the Presence of Other Protein Biogenesis Factors at the Ribosomal Tunnel Exit. J Mol Biol. 431(7):1426-1439.
  21. Srinivasan, K., Dey, S., Sengupta, J. (2019) Structural modules of the stress-induced protein HflX: an outlook on its evolution and biological role. Curr Genet. 65(2):363-370. [Invited review]
  22. Dey, S., Biswas, C., Sengupta, J. (2018) The universally conserved GTPase HflX is an RNA helicase that restores heat-damaged Escherichia coli ribosomes. J Cell Biol. 217(7):2519-2529.
  23. Mahesh, G., Jaiswal, P., Dey, S., Sengupta J, Mukherjee S. (2018) Cloning, Expression, Purification and Characterization of Oligomeric States of the Native 5HT2A G-Protein-Coupled Receptor. Protein Pept Lett. 25(4):390-397.
  24. Pathak, B.K., Banerjee, S., Mondal, S., Chakraborty, B., Sengupta, J., Barat, C. (2017) Unfolded protein exhibits antiassociation activity toward the 50S subunit facilitating 70S ribosome dissociation. FEBS J. 284(22):3915-3930.
  25. Chakraborty, B., Bhakta, S., Sengupta, J. (2016) Mechanistic Insight into the Reactivation of BCAII Enzyme from Denatured and Molten Globule States by Eukaryotic Ribosomes and Domain V rRNAs. PLoS One. 11(4):e0153928.
  26. Chakraborty, B., Sejpal, N.V., Payghan, P.V., Ghoshal, N., Sengupta, J. (2016) Structure-based designing of sordarin derivative as potential fungicide with pan-fungal activity. J Mol Graph Model. 66:133-42.
  27. Shasmal, M., Dey, S., Shaikh, T.R., Bhakta, S., Sengupta, J. (2016) E. coli metabolic protein aldehyde-alcohol dehydrogenase-E binds to the ribosome: a unique moonlighting action revealed. Sci Rep. 6:19936.
  28. Chakraborty, B., Bhakta, S., Sengupta, J. (2016) Disassembly of yeast 80S ribosomes into subunits is a concerted action of ribosome-assisted folding of denatured protein. Biochem Biophys Res Commun. 469(4):923-9.
  29. Chakraborty, B., Mukherjee, R., Sengupta, J. (2013) Structural insights into the mechanism of translational inhibition by the fungicide sordarin. J Comput Aided Mol Des. 27(2):173-84.
  30. Shasmal, M., Sengupta, J. (2012) Structural diversity in bacterial ribosomes: mycobacterial 70S ribosome structure reveals novel features. PLoS One. 7(2):e31742.
  31. Shasmal, M., Chakraborty, B., Sengupta, J. (2010) Intrinsic molecular properties of the protein-protein bridge facilitate ratchet-like motion of the ribosome. Biochem Biophys Res Commun. 399(2):192-7.
  32. Sengupta, J., Bussiere, C., Pallesen, J., West, M., Johnson, A.W., Frank, J. (2010) Characterization of the nuclear export adaptor protein Nmd3 in association with the 60S ribosomal subunit. J Cell Biol. 189(7):1079-86.
  33. Villa, E.*, Sengupta, J.*, Trabuco, L.G., LeBarron, J., Baxter, W.T., Shaikh, T.R., Grassucci, R.A., Nisse,n P., Ehrenberg, M., Schulten, K., Frank, J. (2009)  Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Version 2. Proc Natl Acad Sci U S A. 106(4):1063-8. (*Equal contribution)
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