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. 1989 Apr;86(7):2186–2189. doi: 10.1073/pnas.86.7.2186

Herpes simplex virus 1 helicase-primase: a complex of three herpes-encoded gene products.

J J Crute 1, T Tsurumi 1, L A Zhu 1, S K Weller 1, P D Olivo 1, M D Challberg 1, E S Mocarski 1, I R Lehman 1
PMCID: PMC286876  PMID: 2538835

Abstract

In an earlier report, we described a DNA helicase that is specifically induced upon infection of Vero cells with herpes simplex virus 1. We have purified this enzyme to near homogeneity and found it to consist of three polypeptides with molecular weights of 120,000, 97,000, and 70,000. Immunochemical analysis has shown these polypeptides to be the products of three of the genes UL52, UL5, and UL8 that are required for replication of a plasmid containing a herpes simplex 1 origin (oriS). In addition to helicase activity, the enzyme contains a tightly associated DNA primase. Thus, the three-subunit enzyme is a helicase-primase complex that may prime lagging-strand synthesis as it unwinds DNA at the viral replication fork.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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