Profile
I started my career as a Biophysicist and gradually acquired expertise in Biochemistry and Microbial genetics. My laboratory at CDFD has been operational since December 2001. My major job is to supervise the group, design experiments, and arrange to fund the research activities. The overall objective of my laboratory is to understand the mechanism of transcription elongation, termination, and antitermination in prokaryotes. Recently we have forayed into the synthetic Biology areas. Studies in the following aspects have been in progress in my laboratory for the last five years. a. Mechanism of Rho-dependent termination. b. Physiology of Rho and characterization of Rho-interacting partners. c. Cross-talks between different physiological processes and Rho-dependent termination in vivo. d. Super-resolution microscopy of bacterial transcription proteins. e. Design of anti-Rho peptides using synthetic biology approaches. f. Isolation of novel anti-Mycobacterium proteins from the mycobacteriophage genome. Administrative responsibilities: Served as an In-charge director of CDFD for almost two years in two stints (2016-2017) Served as an In-charge Director of NIAB for a short stint (2016). Served as a full-time Director of DST-IACS, Kolkata for one year (2023-2024).
Current Focus Areas
1) Mechanism and physiology of transcription termination and antitermination processes in E.coli.
2) Synthetic Biology approaches to design peptide antimicrobials..
3) Identifications of novel protein factors from mycobacteriophage genomic libraries capable of modulating the physiological process of Mycobacterium.
Selected Publications
1. Said, N., Hilal, T., Sunday, N. D., Khatri, A., Bürger, J., Mielke, T. Belogurov, G. A., Loll, B., Sen, R., Artsimovitch, I. and Wahl, M. C. (2021). Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ. Science, Jan 1;371(6524): eabd1673.
2. Jain, S., Gupta, R, and Sen, R. (2019) Rho-dependent transcription termination in bacteria recycles RNA polymerases stalled at the DNA lesions. Nature Communications, Mar 14; 10(1):1207. DOI: 10.1038/s41467-019-09146-5..
3. Mitra, P., Ghosh, G., Hafeezunnisa, M., and Sen, R. (2017). Rho protein: mechanism and action. Annual Review of Microbiology, 71, 687-709..
4. Ranjan, A., Banerjee, R., Sharma, S., Sen, U., and Sen, R. (2013). Structural and mechanistic basis of antitermination of Rho-dependent transcription termination by a bacteriophage capsid protein. Nucleic Acids Research, 41 (14):6839-6856..
5. Sen, R., King, R., and Weisberg, R. W. (2001). Modification of the properties of elongating RNA polymerase by persistent association with nascent antiterminator RNA. Molecular Cell. 7(5): 993-1001.