AI Article Synopsis
- The genome of herpes simplex virus type-1 can recombine frequently without a specific viral RecA-type protein.
- Researchers propose that the virus's single strand DNA-binding protein (ICP8) and helicase-primase work together to facilitate this recombination.
- Experiments show that ICP8 forms recombination intermediates and, along with helicase-primase, enhances homologous pairing and branch migration during strand exchange.
Article Abstract
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.
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| http://dx.doi.org/10.1074/jbc.M109988200 | DOI Listing |
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