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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1991 Feb 15;88(4):1105–1109. doi: 10.1073/pnas.88.4.1105

Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products.

M S Dodson 1, I R Lehman 1
PMCID: PMC50965  PMID: 1847509

Abstract

Herpes simplex virus 1 encodes a helicase-primase that is composed of the products of the UL5, UL8, and UL52 genes. A stable subassembly consisting of only the UL5 and UL52 gene products has been purified to near homogeneity from insect cells doubly infected with baculovirus recombinant for these two genes. The purified subassembly has the DNA-dependent ATPase, DNA-dependent GTPase, DNA helicase, and DNA primase activities that are characteristic of the three-subunit holoenzyme. The purified UL8 gene product, although required for viral DNA replication, neither exhibits these enzymatic activities nor stably associates with either the UL5 or the UL52 gene product.

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Selected References

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