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 He, X.
Right arrow Articles by Lehman, I. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by He, X.
Right arrow Articles by Lehman, I. R.

 Previous Article  |  Next Article 

Journal of Virology, June 2000, p. 5726-5728, Vol. 74, No. 12
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Unwinding of a Herpes Simplex Virus Type 1 Origin of Replication (OriS) by a Complex of the Viral Origin Binding Protein and the Single-Stranded DNA Binding Protein

Xiaodun He and I. R. Lehman*

Department of Biochemistry, Stanford University, Stanford, California 94305-5037

Received 14 February 2000/Accepted 29 March 2000

A herpes simplex virus type 1 (HSV-1) OriS analogue in which the A+T sequence linking the box I and II elements was replaced by two single-stranded oligo(dT)s is unwound by the UL9 protein-ICP8 complex. Unwinding of wild-type OriS by the UL9 protein-ICP8 complex was also observed under conditions which destabilize the A+T sequence. These experiments support a model for the unwinding of OriS in which destabilization of the A+T sequence can generate a single-stranded DNA binding site for ICP8, which then associates with the UL9 protein bound to boxes I and II to promote the bidirectional unwinding of OriS.

* Corresponding author. Mailing address: Department of Biochemistry, Beckman Center, Stanford University, Stanford, CA 94305-5037. Phone: (650) 723-6164. Fax: (650) 723-6783. E-mail: blehman{at}cmgm.stanford.edu.

Journal of Virology, June 2000, p. 5726-5728, Vol. 74, No. 12
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Schildgen, O., Graper, S., Blumel, J., Matz, B. (2005). Genome Replication and Progeny Virion Production of Herpes Simplex Virus Type 1 Mutants with Temperature-Sensitive Lesions in the Origin-Binding Protein. J. Virol. 79: 7273-7278 [Abstract] [Full Text]  
  • Colletti, K. S., Xu, Y., Yamboliev, I., Pari, G. S. (2005). Human Cytomegalovirus UL84 Is a Phosphoprotein That Exhibits UTPase Activity and Is a Putative Member of the DExD/H Box Family of Proteins. J. Biol. Chem. 280: 11955-11960 [Abstract] [Full Text]  
  • Trego, K. S., Zhu, Y., Parris, D. S. (2005). The herpes simplex virus type 1 DNA polymerase processivity factor, UL42, does not alter the catalytic activity of the UL9 origin-binding protein but facilitates its loading onto DNA. Nucleic Acids Res 33: 536-545 [Abstract] [Full Text]  
  • Grose, C., Tyler, S., Peters, G., Hiebert, J., Stephens, G. M., Ruyechan, W. T., Jackson, W., Storlie, J., Tipples, G. A. (2004). Complete DNA Sequence Analyses of the First Two Varicella-Zoster Virus Glycoprotein E (D150N) Mutant Viruses Found in North America: Evolution of Genotypes with an Accelerated Cell Spread Phenotype. J. Virol. 78: 6799-6807 [Abstract] [Full Text]  
  • Ma, Y., Wang, T., Villemain, J. L., Giedroc, D. P., Morrical, S. W. (2004). Dual Functions of Single-stranded DNA-binding Protein in Helicase Loading at the Bacteriophage T4 DNA Replication Fork. J. Biol. Chem. 279: 19035-19045 [Abstract] [Full Text]  
  • Trego, K. S., Parris, D. S. (2003). Functional Interaction between the Herpes Simplex Virus Type 1 Polymerase Processivity Factor and Origin-Binding Proteins: Enhancement of UL9 Helicase Activity. J. Virol. 77: 12646-12659 [Abstract] [Full Text]  
  • Makhov, A. M., Lee, S. S.-K., Lehman, I. R., Griffith, J. D. (2003). Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: Visualization of a specific preunwinding complex. Proc. Natl. Acad. Sci. USA 100: 898-903 [Abstract] [Full Text]  
  • Aslani, A., Olsson, M., Elias, P. (2002). ATP-dependent Unwinding of a Minimal Origin of DNA Replication by the Origin-binding Protein and the Single-strand DNA-binding Protein ICP8 from Herpes Simplex Virus Type I. J. Biol. Chem. 277: 41204-41212 [Abstract] [Full Text]  
  • Cohrs, R. J., Wischer, J., Essman, C., Gilden, D. H. (2002). Characterization of Varicella-Zoster Virus Gene 21 and 29 Proteins in Infected Cells. J. Virol. 76: 7228-7238 [Abstract] [Full Text]  
  • Tanguy Le Gac, N., Boehmer, P. E. (2002). Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins. J. Biol. Chem. 277: 5660-5666 [Abstract] [Full Text]  
  • He, X., Lehman, I. R. (2001). An initial ATP-independent step in the unwinding of a herpes simplex virus type I origin of replication by a complex of the viral origin-binding protein and single-strand DNA-binding protein. Proc. Natl. Acad. Sci. USA 10.1073/pnas.061028298v1 [Abstract] [Full Text]  
  • Arana, M. E., Haq, B., Tanguy Le Gac, N., Boehmer, P. E. (2001). Modulation of the Herpes Simplex Virus Type-1 UL9 DNA Helicase by Its Cognate Single-strand DNA-binding Protein, ICP8. J. Biol. Chem. 276: 6840-6845 [Abstract] [Full Text]  
  • Marintcheva, B., Weller, S. K. (2001). Residues within the Conserved Helicase Motifs of UL9, the Origin-binding Protein of Herpes Simplex Virus-1, Are Essential for Helicase Activity but Not for Dimerization or Origin Binding Activity. J. Biol. Chem. 276: 6605-6615 [Abstract] [Full Text]  
  • He, X., Lehman, I. R. (2001). An initial ATP-independent step in the unwinding of a herpes simplex virus type I origin of replication by a complex of the viral origin-binding protein and single-strand DNA-binding protein. Proc. Natl. Acad. Sci. USA 98: 3024-3028 [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»