Syam P. Anand, Ph.D.
University of Pittsburgh Laboratory of Physical Molecular Biology
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Syam P. Anand, Ph.D.
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 Postdoctoral Research Associate in the laboratory of Professor Saleem Khan in the Department of Molecular Genetics and Biochemistry. With Saleem, I have shown that PcrA helicase is structure-specific and has both 3'?5' and 5'? 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. Haocheng and I are working closely, and 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).
 
   
   
   
 

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