Protein Engineering, Post-translational modification analysis, Mass spectrometry, Directed evolution.
Our group holds interest in tinkering with and exploring the post-translational modifications of proteins namely glycosylation and N- α acetylation, in bacteria. At CSIR-IMTECH, we have successfully developed methods for protein O- and S- glycosylation and currently we are endeavouring to develop a versatile tool-kit for efficient glycosylation/acetylation of proteins or peptides for useful applications. A parallel research interest of our group is to understand the biological significance of these modifications in cellular context, more specifically in M. tuberculosis pathogenesis. In sync with CSIR-Spirit, we actively collaborate with industry and have ongoing association with partners namely Revelations Biotech Pvt. Ltd., and Premas Biotech Pvt. Ltd. In past, our association with Criyagen Agri and Biotech Pvt. Ltd. led to a successful market launch of a growth promoting product for crop applications.
- Nagar, R., and Rao, A. (2017) An iterative glycosyltransferase EntS catalyzes transfer and extension of O- and S-linked monosaccharide in enterocin 96. Glycobiology. 10.1093/glycob/cwx042.
- Bhat, A. H., Pathak, D., and Rao, A. (2017) The alr-groEL1 operon in Mycobacterium tuberculosis: an interplay of multiple regulatory elements. Scientific Reports. 7, 43772.
- MPathak, D., Bhat, A. H., Sapehia, V., Rai, J., and Rao, A. (2016) Biochemical evidence for relaxed substrate specificity of Nα-acetyltransferase (Rv3420c/rimI) of Mycobacterium tuberculosis. Scientific Reports. 10.1038/srep28892.
- Bhat, A. H., Mondal, H., Chauhan, J. S., Raghava, G. P. S., Methi, A., and Rao, A. (2011) ProGlycProt: a repository of experimentally characterized prokaryotic glycoproteins. Nucleic Acids Research. 10.1093/nar/gkr911.
- Rao, A., Chopra, S., Ram, G., Gupta, A., and Ranganathan, A. (2005) Application of the “Codon-shuffling” Method. Journal of Biological Chemistry. 280, 23605–23614.