Dr. Sharada

Post Doctoral Fellow
Academic Profile
Doctoral Degree:Dept of Biochemistry, Central college, Bangalore University, Bangalore.
Post Graduation:Dept of Biochemistry, Central college, Bangalore University, Bangalore.
Project Title:Deciphering the functions of Mycobacterium tuberculosis nucleoid-associated proteins.

Bacterial nucleoid is a dynamic entity consisting of DNA genome and associated proteins (Nucleoid Associated Proteins; NAPs) , which influence not only the DNA conformation, but a range of processes like DNA replication, recombination, repair and gene regulation. Some of the nucleoid associated proteins, like H-NS (histone-like nucleoid-structuring protein), influence the expression of many genes including those related to environmental adaptation and also the virulence factors encoded by horizontally acquired DNA. The nucleoid structure is constantly remodelled by these proteins in response to environmental signals and/or growth conditions. My research aims in understanding the functions of nucleoid-associated proteins in Mycobacterium tuberculosis, which helps in better understanding of the modulation of the mycobacterial genomic landscape and the DNA transactions leading to the virulence of this elusive pathogen.

  • Sharadamma, N., Harshavardhana, Y., Ravishankar, A., Anand, P., Chandra, N., and Muniyappa, K. (2015). Molecular Dissection of Mycobacterium tuberculosis Integration Host Factor Reveals Novel Insights into the Mode of DNA Binding and Nucleoid Compaction. Biochemistry 54, 4142-4160. | Pubmed
  • Sharadamma, N., Khan, K., Kumar, S., Neelakanteshwar Patil, K., Hasnain, S.E., and Muniyappa, K. (2011). Synergy between the N- and C-terminal Domains of Mycobacterium tuberculosis HupB is Essential for High-affinity Binding, DNA Supercoiling and Inhibition of RecA-promoted Strand Exchange. FEBS J. | Pubmed
  • Sharadamma, N., Harshavardhana, Y., Singh, P., and Muniyappa, K. (2010). Mycobacterium tuberculosis nucleoid-associated DNA-binding protein H-NS binds with high-affinity to the Holliday junction and inhibits strand exchange promoted by RecA protein. Nucleic Acids Res 38, 3555-3569. | Pubmed