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J Biol Chem, Vol. 275, Issue 8, 5880-5887, February 25, 2000
From the Department of Medical Biochemistry, Göteborg
University, Box 440, SE 405 30 Göteborg, Sweden
The Herpes simplex virus type I origin binding
protein (OBP) is a sequence-specific DNA-binding protein and a dimeric
DNA helicase encoded by the UL9 gene. It is required for the activation of the viral origin of DNA replication oriS. Here we demonstrate that
the linear double-stranded form of oriS can be converted by heat
treatment to a stable novel conformation referred to as oriS*. Studies
using S1 nuclease suggest that oriS* consists of a central hairpin with
an AT-rich sequence in the loop. Single-stranded oligonucleotides
corresponding to the upper strand of oriS can adopt the same structure.
OBP forms a stable complex with oriS*. We have identified structural
features of oriS* recognized by OBP. The central oriS palindrome as
well as sequences at the 5' side of the oriS palindrome were required
for complex formation. Importantly, we found that mutations that have
been shown to reduce oriS-dependent DNA replication also
reduce the formation of the OBP-oriS* complex. We suggest that oriS*
serves as an intermediate in the initiation of DNA replication
providing the initiator protein with structural information for a
selective and efficient assembly of the viral replication machinery.
A Novel Conformation of the Herpes Simplex Virus Origin of DNA
Replication Recognized by the Origin Binding Protein*
*
This work was supported by Swedish Cancer Society Grant
2552-B99-13XCC and the Swedish Foundation for Strategic Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 46-31-7733486;
Fax: 46-31-416108; E-mail: per.elias@medkem.gu.se.
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