JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on October 18, 2002
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
277/43/41204    most recent
M208270200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Aslani, A.
Right arrow Articles by Elias, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Aslani, A.
Right arrow Articles by Elias, P.
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?

Papers In Press, published online ahead of print August 14, 2002
J. Biol. Chem, 10.1074/jbc.M208270200
Submitted on August 13, 2002
Revised on August 14, 2002
Accepted on August 14, 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

Alireza Aslani, Monica Olsson, and Per Elias

Medical Biochemistry, Goteborg University, Goteborg SE 405 30

Corresponding Author: per.elias{at}medkem.gu.se

The Herpes simplex virus type I origin binding protein, OBP, is encoded by the UL9 gene. OBP binds the origin of DNA replication, oriS, in a cooperative and sequence specific manner. OBP is also an ATP dependent DNA helicase. We have recently shown that single-stranded oriS folds into a unique and evolutionarily conserved conformation, oriS*, which is stably bound by OBP. OriS* is contains a stable hairpin formed by complementary base-pairing between box I and box III in oriS. Here we show that OBP, in the presence of the single-strand DNA binding protein ICP8, can convert an 80 base pair double-stranded minimal oriS fragment to oriS* and form an OBP/oriS* complex. The formation of an OBP/oriS* complex requires hydrolysable ATP. We also demonstrate that OBP in the presence of ICP8 and ATP promotes slow but specific and complete unwinding of duplex minimal oriS. The possibility that the OBP/oriS* complex may serve as an assembly site for the herpes virus replisome is discussed.


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. 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. V. Nimonkar and P. E. Boehmer
Reconstitution of recombination-dependent DNA synthesis in herpes simplex virus 1
PNAS, September 2, 2003; 100(18): 10201 - 10206.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.