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J. Biol. Chem., Vol. 277, Issue 43, 41204-41212, October 25, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/43/41204    most recent M208270200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Aslani, A. Articles by Elias, P. Search for Related Content PubMed PubMed Citation Articles by Aslani, A. Articles by Elias, P. Social Bookmarking                      What's this?

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

From the Department of Medical Biochemistry, Göteborg University, Box 440, SE 405 30 Göteborg University, Sweden

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* 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-stranded 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.

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