Syam P. Anand, Ph.D.

I am a Research Instructor in the laboratory of Professor Saleem Khan in the Department of Microbiology and Molecular Genetics. My long-term objective is to understand the molecular mechanisms that regulate the activity of motor proteins. Motor proteins accelerate cellular processes by overcoming the limits and barriers imposed by diffusion and Brownian motion. They accomplish this by converting chemical energy into mechanical energy in a variety of different scenarios. Of particular interest to me are the motor proteins that carry out DNA transactions in pathogenic bacteria. With Saleem, I have shown that PcrA helicase is structure-specific and has both 3'→5' and 5'→3' helicase activities. As part of a collaborative study between the Khan and Leuba laboratories, I have been utilizing single-molecule approaches to study the mechanism of action of helicases. Recently, we have shown that PcrA helicase displaces the recombination protein RecA from DNA. Moreover, we also showed that the helicase activity of the protein is not essential for this function. We are working closely, combining both biochemical and single-molecule techniques to discover the precise activities of helicases.




	Syam P. Anand, Ph.D. B.Sc. Botany, Calicut University, India M.Sc., Microbiology, Mahatma Gandhi University, India Ph.D., Molecular Biology and Biochemistry, Indian Institute of Science, India

		I am a Research Instructor in the laboratory of Professor Saleem Khan in the Department of Microbiology and Molecular Genetics. My long-term objective is to understand the molecular mechanisms that regulate the activity of motor proteins. Motor proteins accelerate cellular processes by overcoming the limits and barriers imposed by diffusion and Brownian motion. They accomplish this by converting chemical energy into mechanical energy in a variety of different scenarios. Of particular interest to me are the motor proteins that carry out DNA transactions in pathogenic bacteria. With Saleem, I have shown that PcrA helicase is structure-specific and has both 3'→5' and 5'→3' helicase activities. As part of a collaborative study between the Khan and Leuba laboratories, I have been utilizing single-molecule approaches to study the mechanism of action of helicases. Recently, we have shown that PcrA helicase displaces the recombination protein RecA from DNA. Moreover, we also showed that the helicase activity of the protein is not essential for this function. We are working closely, combining both biochemical and single-molecule techniques to discover the precise activities of helicases.


Selected Publications
Anilkumar, G., Srinivasan, R., Anand, S. P. and Ajitkumar, P. Bacterial cell division protein FtsZ is a specific substrate for the AAA family protease FtsH. Microbiology 147, 516-517 (2001). Chang, T. L., Naqvi, A., Anand, S. P., Kramer, M. G., Munshi, R. and Khan, S. A. Biochemical characterization of the staphylococcus aureus PcrA helicase and its role in plasmid rolling-circle replication. J. Biol. Chem. 277, 45880-45886 (2002). Anand, S. P., Mitra, P., Naqvi, A. and Khan, S. A. Bacillus anthracis and Bacillus cereus PcrA helicases can support DNA unwinding and in vitro rolling-circle replication of plasmid pT181 of Staphylococcus aureus. J. Bacteriol. 186, 2195-2199 (2004). Anand, S. P., Rajeswari, H., Gupta, P., Srinivasan, R., Indi, S. and Ajitkumar, P. A C-terminal deletion mutant of Mycobacterium tuberculosis FtsZ shows fast polymerization in vitro. Microbiology 150, 1119-1121 (2004). Anand, S. P. and Khan, S. A. Structure-specific DNA binding and bipolar helicase activities of PcrA. Nucleic Acids Res. 32, 3190-3197 (2004). Anand, S. P., Chattopadhyay, A. and Khan, S. A. The PcrA3 mutant binds DNA and interacts with the RepC initiator protein but is defective in its DNA helicase and unwinding activities. Plasmid 54, 104-113 (2005). Anand, S. P., Zheng, H., Bianco, P., Leuba, S. H. and Khan, S. A. DNA helicase activity of PcrA is not required for the displacement of RecA from DNA and inhibition of RecA-mediated strand exchange. J. Bacteriology 189, 4502-4509, 2007. Anand, S. P., Akhtar, P., Tinsley, E., Watkins, S. C. and Khan, S. A. GTP-dependent polymerization of the tubulin-like RepX replication initiation protein encoded by the pXO1 plasmid of B. anthracis. Mol. Microbiol. 2008, 67:881-890. *Both authors contributed equally to the work.