This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kumar, A.
Right arrow Articles by Bullock, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kumar, A.
Right arrow Articles by Bullock, P. A.

 Previous Article  |  Next Article 

Journal of Virology, May 2007, p. 4808-4818, Vol. 81, No. 9
0022-538X/07/$08.00+0     doi:10.1128/JVI.02451-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

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{triangledown}

Anuradha Kumar,1 Gretchen Meinke,1 Danielle K. Reese,1 Stephanie Moine,1 Paul J. Phelan,1 Amélie Fradet-Turcotte,2 Jacques Archambault,2 Andrew Bohm,1 and Peter A. Bullock1*

Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111,1 Institut de Recherches Cliniques de Montreal, 110 Avenue des Pins Ouest, Montreal, Quebec, Canada H2W 1R72

Received 7 November 2006/ Accepted 30 January 2007

The interaction of simian virus 40 (SV40) T antigen (T-ag) with the viral origin has served as a model for studies of site-specific recognition of a eukaryotic replication origin and the mechanism of DNA unwinding. These studies have revealed that a motif termed the "beta-hairpin" is necessary for assembly of T-ag on the SV40 origin. Herein it is demonstrated that residues at the tip of the "beta-hairpin" are needed to melt the origin-flanking regions and that the T-ag helicase domain selectively assembles around one of the newly generated single strands in a manner that accounts for its 3'-to-5' helicase activity. Furthermore, T-ags mutated at the tip of the "beta-hairpin" are defective for oligomerization on duplex DNA; however, they can assemble on hybrid duplex DNA or single-stranded DNA (ssDNA) substrates provided the strand containing the 3' extension is present. Collectively, these experiments indicate that residues at the tip of the beta-hairpin generate ssDNA in the core origin and that the ssDNA is essential for subsequent oligomerization events.

* 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 7 February 2007.

Journal of Virology, May 2007, p. 4808-4818, Vol. 81, No. 9
0022-538X/07/$08.00+0     doi:10.1128/JVI.02451-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kwun, H. J., Guastafierro, A., Shuda, M., Meinke, G., Bohm, A., Moore, P. S., Chang, Y. (2009). The Minimum Replication Origin of Merkel Cell Polyomavirus Has a Unique Large T-Antigen Loading Architecture and Requires Small T-Antigen Expression for Optimal Replication. J. Virol. 83: 12118-12128 [Abstract] [Full Text]  
  • 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]  
  • Kumar, A., Joo, W. S., Meinke, G., Moine, S., Naumova, E. N., Bullock, P. A. (2008). Evidence for a Structural Relationship between BRCT Domains and the Helicase Domains of the Replication Initiators Encoded by the Polyomaviridae and Papillomaviridae Families of DNA Tumor Viruses. J. Virol. 82: 8849-8862 [Abstract] [Full Text]  
  • Ozaki, S., Kawakami, H., Nakamura, K., Fujikawa, N., Kagawa, W., Park, S.-Y., Yokoyama, S., Kurumizaka, H., Katayama, T. (2008). A Common Mechanism for the ATP-DnaA-dependent Formation of Open Complexes at the Replication Origin. J. Biol. Chem. 283: 8351-8362 [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]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»