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Journal of Virology, December 2006, p. 12248-12259, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01201-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Analyses of the Interaction between the Origin Binding Domain from Simian Virus 40 T Antigen and Single-Stranded DNA Provide Insights into DNA Unwinding and Initiation of DNA Replication{triangledown}

Danielle K. Reese,{dagger} Gretchen Meinke,{dagger} Anuradha Kumar,{dagger} Stephanie Moine, Kathleen Chen, James L. Sudmeier, William Bachovchin, Andrew Bohm, and Peter A. Bullock*

Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 8 June 2006/ Accepted 12 September 2006

DNA helicases are essential for DNA metabolism; however, at the molecular level little is known about how they assemble or function. Therefore, as a model for a eukaryotic helicase, we are analyzing T antigen (T-ag) the helicase encoded by simian virus 40. In this study, nuclear magnetic resonance (NMR) methods were used to investigate the transit of single-stranded DNA (ssDNA) through the T-ag origin-binding domain (T-ag OBD). When the residues that interact with ssDNA are viewed in terms of the structure of a hexamer of the T-ag OBD, comprised of residues 131 to 260, they indicate that ssDNA passes over one face of the T-ag OBD and then transits through a gap in the open ring structure. The NMR-based conclusions are supported by an analysis of previously described mutations that disrupt critical steps during the initiation of DNA replication. These and related observations are discussed in terms of the threading of DNA through T-ag hexamers and the initiation of viral DNA replication.

* Corresponding author. Mailing address: Department of Biochemistry A703, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Phone: (617) 636-0447. Fax: (617) 636-2409. E-mail: peter.bullock{at}tufts.edu.

{triangledown} Published ahead of print on 27 September 2006.

{dagger} D.K.R., G.M., and A.K. contibuted equally to this work.

Journal of Virology, December 2006, p. 12248-12259, Vol. 80, No. 24
0022-538X/06/$08.00+0     doi:10.1128/JVI.01201-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wang, W., Simmons, D. T. (2009). Simian Virus 40 Large T Antigen Can Specifically Unwind the Central Palindrome at the Origin of DNA Replication. J. Virol. 83: 3312-3322 [Abstract] [Full Text]  
  • Fradet-Turcotte, A., Vincent, C., Joubert, S., Bullock, P. A., Archambault, J. (2007). Quantitative Analysis of the Binding of Simian Virus 40 Large T Antigen to DNA. J. Virol. 81: 9162-9174 [Abstract] [Full Text]  
  • Kumar, A., Meinke, G., Reese, D. K., Moine, S., Phelan, P. J., Fradet-Turcotte, A., Archambault, J., Bohm, A., Bullock, P. A. (2007). Model for T-Antigen-Dependent Melting of the Simian Virus 40 Core Origin Based on Studies of the Interaction of the Beta-Hairpin with DNA. J. Virol. 81: 4808-4818 [Abstract] [Full Text]  
  • Wang, W., Manna, D., Simmons, D. T. (2007). Role of the Hydrophilic Channels of Simian Virus 40 T-Antigen Helicase in DNA Replication. J. Virol. 81: 4510-4519 [Abstract] [Full Text]  


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