JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lee, S. S. K.
Right arrow Articles by Lehman, I. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lee, S. S. K.
Right arrow Articles by Lehman, I. R.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 274, Issue 26, 18613-18617, June 25, 1999

The Interaction of Herpes Simplex Type 1 Virus Origin-binding Protein (UL9 Protein) with Box I, the High Affinity Element of the Viral Origin of DNA Replication

Sam S. K. Lee and I. R. Lehman

From the Department of Biochemistry, Beckman Center, Stanford University, Stanford, California 94305-5307

The herpes simplex type 1 (HSV-1) origin binding protein, the UL9 protein, exists in solution as a homodimer of 94-kDa monomers. It binds to Box I, the high affinity element of the HSV-1 origin, Oris, as a dimer. The UL9 protein also binds the HSV-1 single strand DNA-binding protein, ICP8. Photocross-linking studies have shown that although the UL9 protein binds Box I as a dimer, only one of the two monomers contacts Box I. It is this form of the UL9 homodimer that upon interaction with ICP8, promotes the unwinding of Box I coupled to the hydrolysis of ATP to ADP and Pi. Photocross-linking studies have also shown that the amount of UL9 protein that interacts with Box I is reduced by its interaction with ICP8.

Antibody directed against the C-terminal ten amino acids of the UL9 protein inhibits its Box I unwinding activity, consistent with the requirement for interaction of the C terminus of the UL9 protein with ICP8. Inhibition by the antibody is enhanced when the UL9 protein is first bound to Box I, suggesting that the C terminus of the UL9 protein undergoes a conformational change upon binding Box I.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
K. S. Trego, Y. Zhu, and D. S. Parris
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., January 26, 2005; 33(2): 536 - 545.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Macao, M. Olsson, and P. Elias
Functional Properties of the Herpes Simplex Virus Type I Origin-binding Protein Are Controlled by Precise Interactions with the Activated Form of the Origin of DNA Replication
J. Biol. Chem., July 9, 2004; 279(28): 29211 - 29217.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
K. S. Trego and D. S. Parris
Functional Interaction between the Herpes Simplex Virus Type 1 Polymerase Processivity Factor and Origin-Binding Proteins: Enhancement of UL9 Helicase Activity
J. Virol., December 1, 2003; 77(23): 12646 - 12659.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. M. Makhov, S. S.-K. Lee, I. R. Lehman, and J. D. Griffith
Origin-specific unwinding of herpes simplex virus 1 DNA by the viral UL9 and ICP8 proteins: Visualization of a specific preunwinding complex
PNAS, February 4, 2003; 100(3): 898 - 903.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
N. Tanguy Le Gac and P. E. Boehmer
Activation of the Herpes Simplex Virus Type-1 Origin-binding Protein (UL9) by Heat Shock Proteins
J. Biol. Chem., February 8, 2002; 277(7): 5660 - 5666.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
L. T. Krug, N. Inoue, and P. E. Pellett
Sequence Requirements for Interaction of Human Herpesvirus 7 Origin Binding Protein with the Origin of Lytic Replication
J. Virol., April 15, 2001; 75(8): 3925 - 3936.
[Abstract] [Full Text]

Home page
 J. Virol.Home page
M. Mapelli, M. Mühleisen, G. Persico, H. van der Zandt, and P. A. Tucker
The 60-Residue C-Terminal Region of the Single-Stranded DNA Binding Protein of Herpes Simplex Virus Type 1 Is Required for Cooperative DNA Binding
J. Virol., October 1, 2000; 74(19): 8812 - 8822.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
A. Aslani, S. Simonsson, and P. Elias
A Novel Conformation of the Herpes Simplex Virus Origin of DNA Replication Recognized by the Origin Binding Protein
J. Biol. Chem., February 25, 2000; 275(8): 5880 - 5887.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. B. Murata and M. S. Dodson
The Herpes Simplex Virus Type 1 Origin-binding Protein. SEQUENCE-SPECIFIC ACTIVATION OF ADENOSINE TRIPHOSPHATASE ACTIVITY BY A DOUBLE-STRANDED DNA CONTAINING BOX I
J. Biol. Chem., December 24, 1999; 274(52): 37079 - 37086.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
I. R. Lehman and P. E. Boehmer
Replication of Herpes Simplex Virus DNA
J. Biol. Chem., October 1, 1999; 274(40): 28059 - 28062.
[Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.