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J. Biol. Chem., Vol. 277, Issue 17, 15182-15189, April 26, 2002
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From the Department of Biochemistry and Molecular Biology,
University of Miami School of Medicine, Miami, Florida 33101-6129
The genome of herpes simplex virus type-1
undergoes a high frequency of homologous recombination in the absence
of a virus-encoded RecA-type protein. We hypothesized that viral
homologous recombination is mediated by the combined action of the
viral single strand DNA-binding protein (ICP8) and helicase-primase.
Our results show that ICP8 catalyzes the formation of recombination
intermediates (joint molecules) between circular single-stranded
acceptor and linear duplex donor DNA. Joint molecules formed by
invasion of a 3'-terminal strand displaces the non-complementary
5'-terminal strand, thereby creating a loading site for the
helicase-primase. Helicase-primase acts on these joint molecules to
promote ATP-dependent branch migration. Finally, we have
reconstituted strand exchange by the synchronous action of ICP8 and
helicase-primase. Based on these data, we present a recombination
mechanism for a eukaryotic DNA virus in which a single strand
DNA-binding protein and helicase cooperate to promote homologous
pairing and branch migration.
In Vitro Strand Exchange Promoted by the Herpes
Simplex Virus Type-1 Single Strand DNA-binding Protein (ICP8)
and DNA Helicase-Primase*
*
This work was supported by National Institutes of Health
Grant GM62643 and Florida Biomedical Research Program Grant BM 022.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: Dept. of Biochemistry
and Molecular Biology, University of Miami School of Medicine, P. O.
Box 016129, Miami, FL 33101-6129. Tel.: 305-243-2934; Fax: 305-243-3955; E-mail: pboehmer@molbio.med.miami.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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