Office: 843-792-0281
Lab: 843-792-0281
Fax: 843-792-8568
Email: mohanty@musc.edu
BSB-517

Research Interests

II. DNA replication arrest-dependent homologous recombination

Our long-term goal is to understand genome integrity using the budding yeast Saccharomyces cerevisiae as a model. One of the current projects is to understand how programmed replication arrest products are processed by the homologous recombination. Our present interest is to identify all the factors that are involved in the replication arrest-dependent recombination and understand their mechanism of action.

Selected Publications

• Mohanty, B. K, Bairwa, N. K, and Bastia, D. (2009) Contrasting Roles of Checkpoint Proteins as Recombination Modulators At Fob1-Ter Complexes With or Without Fork Arrest. Eukaryot Cell. In press.
• Matmati, N., Kitagaki, H., Montefusco, D., Mohanty, B. K and Hannun, Y. A. (2009) Hydroxyurea sensitivity reveals a role for ISC1 in the regulation of G2/M. J Biol Chem. 2009 Jan 21. [Epub ahead of print]
• Mohanty, B. K., B. K., Bairwa, N. K. and Bastia , D. (2006) The Tof1p-Csm3p protein complex counteracts the Rrm3p helicase to control replication termination of Saccharomyces cerevisiae. Proceedings of National Academy of Sciences U S A . 103 : 897-902.
• Bastia , D. and Mohanty, B. K. (2006) Termination of DNA Replication. DNA replication and human disease (ed. M.L. DePamphilis), pp. 155-174. Cold Spring Harbor Laboratory Press, Cold Spring Harbor , New York .
• Mohanty, B. K. and Bastia , D. (2004) Binding of the Replication Terminator Protein Fob1p to the Ter sites of Yeast Causes Polar Fork Arrest . Journal of Biological Chemistry279 : 1932-1941.
• Mohanty, B. K., Bussiere, D. E., Sahoo, T., Pai, K. S., Meijer, W. J., Bron, S. and Bastia, D. (2001) Structural and functional analysis of a bipolar replication terminus: Implications for the origin of polarity of fork arrest. Journal of Biological Chemistry 276 : 13160-13168.
• Mohanty, B. K., Sahoo, T. and Bastia, D. (1998) Mechanistic studies on the impact of transcription on sequence-specific termination of DNA replication and vice versa. Journal of Biological Chemistry 273 : 3051-3059.
• Mohanty, B. K., Sahoo, T., Bastia, D. (1996) The relationship between sequence-specific termination of DNA replication and transcription. EMBO Journal 15 : 2530-2539.
• Ratnakar, P. V. A. L., Mohanty, B. K., Lobert, M. and Bastia, D. (1996) The replication initiator protein p of the plasmid R6K specifically interacts with the host-encoded helicase DnaB. Proceedings of National Academy of Sciences U S A. 93 : 5522-5526.
• Lu, YB, Ratnakar, P. V. A. L., Mohanty, B. K, and Bastia, D. (1996) Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA. Proceedings of National Academy of Sciences U S A. 93 : 12902-12907.
• Bastia, D. and Mohanty, B. K. (1996) Mechanisms for completing DNA replication. In DNA Replication in Eukaryotic Cells. (Ed. DePamphilis. M. L.) Cold Spring Harbor Laboratory Press, NY. pp: 177-215.
• Sahoo T, Mohanty BK, Patel I, Bastia D. (1995) Termination of DNA replication in vitro: requirement for stereospecific interaction between two dimers of the replication terminator protein of Bacillus subtilis and with the terminator site to elicit polar contrahelicase and fork impedance. EMBO Journal 14 : 619-628.
• Sahoo, T., Mohanty, B. K., Lobert, M., Manna, A. C. and Bastia, D. (1995) The contrahelicase activities of the replication terminator proteins of Escherichia coli and Bacillus subtilis are helicase-specific and impede both helicase translocation and authentic DNA unwinding. Journal of Biological Chemistry 270 : 29138-29144.
• Kaul, S., Mohanty, B. K., Sahoo, T., Patel, I., Khan, S. A. and Bastia, D. (1994) The replication terminator protein of the gram-positive bacterium Bacillus subtilis functions as a polar contrahelicase in gram-negative Escherichia coli. Proceedings of National Academy of Sciences U S A. 91 : 11143-11147.
• Mohanty, B. K., Krishna, B. M and Das, M. R. (1993) A novel way to generate nonspecifically radiolabeled proteins for use as molecular-weight markers. Journal of Biochemical Biophysical Methods 27 : 267-279.