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Papers In Press, published online ahead of print February 6, 2002
Department of Biochemistry and Molecular Biology (R-629), University of Miami School of Medicine, Miami, FL 33101-6129
Corresponding Author: pboehmer{at}molbio.med.miami.edu
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.
J. Biol. Chem, 10.1074/jbc.M109988200
Submitted on October 16, 2001
Revised on February 6, 2002
Accepted on February 5, 2002
In vitro strand-exchange promoted by the herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) and DNA helicase-primase
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