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 Sreekumar, K. R.
Right arrow Articles by Bullock, P. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sreekumar, K. R.
Right arrow Articles by Bullock, P. A.

 Previous Article  |  Next Article 

Journal of Virology, September 2000, p. 8589-8600, Vol. 74, No. 18
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Simian Virus 40 Core Origin Contains Two Separate Sequence Modules That Support T-Antigen Double-Hexamer Assembly

K. R. Sreekumar,dagger Andrea E. Prack, Danielle R. Winters, Brett A. Barbaro, and Peter A. Bullock*

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

Received 10 April 2000/Accepted 14 June 2000

Using subfragments of the simian virus 40 (SV40) core origin, we demonstrate that two alternative modules exist for the assembly of T-antigen (T-ag) double hexamers. Pentanucleotides 1 and 3 and the early palindrome (EP) constitute one assembly unit, while pentanucleotides 2 and 4 and the AT-rich region constitute a second, relatively weak, assembly unit. Related studies indicate that on the unit made up of pentanucleotide 1 and 3 and the EP assembly unit, the first hexamer forms on pentanucleotide 1 and that owing to additional protein-DNA and protein-protein interactions, the second hexamer is able to form on pentanucleotide 3. Oligomerization on the unit made up of pentanucleotide 2 and 4 and the AT-rich region is initiated by assembly of a hexamer on pentanucleotide 4; subsequent formation of the second hexamer takes place on pentanucleotide 2. Given that oligomerization on the SV40 origin is limited to double-hexamer formation, it is likely that only a single module is used for the initial assembly of T-ag double hexamers. Finally, we discuss the evidence that nucleotide hydrolysis is required for the remodeling events that result in the utilization of the second assembly unit.

* 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: PBULLOCK{at}OPAL.TUFTS.EDU.

dagger Present address: National Center for Biotechnology Information, National Institutes of Health, Bethesda, MD 20894.

Journal of Virology, September 2000, p. 8589-8600, Vol. 74, No. 18
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • 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]  
  • Meinke, G., Bullock, P. A., Bohm, A. (2006). Crystal Structure of the Simian Virus 40 Large T-Antigen Origin-Binding Domain. J. Virol. 80: 4304-4312 [Abstract] [Full Text]  
  • Reese, D. K., Sreekumar, K. R., Bullock, P. A. (2004). Interactions Required for Binding of Simian Virus 40 T Antigen to the Viral Origin and Molecular Modeling of Initial Assembly Events. J. Virol. 78: 2921-2934 [Abstract] [Full Text]  
  • Simmons, D. T., Gai, D., Parsons, R., Debes, A., Roy, R. (2004). Assembly of the replication initiation complex on SV40 origin DNA. Nucleic Acids Res 32: 1103-1112 [Abstract] [Full Text]  
  • Jiao, J., Simmons, D. T. (2003). Nonspecific Double-Stranded DNA Binding Activity of Simian Virus 40 Large T Antigen Is Involved in Melting and Unwinding of the Origin. J. Virol. 77: 12720-12728 [Abstract] [Full Text]  
  • Titolo, S., Welchner, E., White, P. W., Archambault, J. (2003). Characterization of the DNA-Binding Properties of the Origin-Binding Domain of Simian Virus 40 Large T Antigen by Fluorescence Anisotropy. J. Virol. 77: 5512-5518 [Abstract] [Full Text]  
  • Kim, R. J., Moine, S., Reese, D. K., Bullock, P. A. (2002). Peptides Containing Cyclin/Cdk-Nuclear Localization Signal Motifs Derived from Viral Initiator Proteins Bind to DNA When Unphosphorylated. J. Virol. 76: 11785-11792 [Abstract] [Full Text]  
  • Uhlmann-Schiffler, H., Seinsoth, S., Stahl, H. (2002). Preformed hexamers of SV40 T antigen are active in RNA and origin-DNA unwinding. Nucleic Acids Res 30: 3192-3201 [Abstract] [Full Text]  
  • Purviance, J. D., Prack, A. E., Barbaro, B., Bullock, P. A. (2001). In the Simian Virus 40 In Vitro Replication System, Start Site Selection by the Polymerase {alpha}-Primase Complex Is Not Significantly Altered by Changes in the Concentration of Ribonucleotides. J. Virol. 75: 6392-6401 [Abstract] [Full Text]  
  • Barbaro, B. A., Sreekumar, K. R., Winters, D. R., Prack, A. E., Bullock, P. A. (2000). Phosphorylation of Simian Virus 40 T Antigen on Thr 124 Selectively Promotes Double-Hexamer Formation on Subfragments of the Viral Core Origin. J. Virol. 74: 8601-8613 [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»