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. 1995 Aug 15;92(17):7882-6.
doi: 10.1073/pnas.92.17.7882.

Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha

S S Lee  1 , Q Dong, T S Wang, I R Lehman
Affiliations

Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha

S S Lee et al. Proc Natl Acad Sci U S A. .

Abstract

The herpes simplex virus 1 (HSV-1) genome encodes seven polypeptides that are required for its replication. These include a heterodimeric DNA polymerase, a single-strand-DNA-binding protein, a heterotrimeric helicase/primase, and a protein (UL9 protein) that binds specifically to an HSV-1 origin of replication (oris). We demonstrate here that UL9 protein interacts specifically with the 180-kDa catalytic subunit of the cellular DNA polymerase alpha-primase. This interaction can be detected by immunoprecipitation with antibodies directed against either of these proteins, by gel mobility shift of an oris-UL9 protein complex, and by stimulation of DNA polymerase activity by the UL9 protein. These findings suggest that enzymes required for cellular DNA replication also participate in HSV-1 DNA replication.

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