The UL8 subunit of the herpes simplex virus type-1 DNA helicase-primase optimizes utilization of DNA templates covered by the homologous single- strand DNA-binding protein ICP8

Nicolas Tanguy Le Gac, Giuseppe Villani, Jean Sébastien Hoffmann, Paul E Boehmer

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The herpes simplex virus type-1 DNA helicase-primase is a heterotrimer encoded by the UL5, UL8, and UL52 genes. The core enzyme, specified by the UL5 and UL52 genes, retains DNA helicase, DNA-dependent nucleoside triphospbatase, and primase activities. The UL8 subunit has previously been implicated in increasing primer stability and in stimulating primer synthesis by the core enzyme. To further characterize the function of the UL8 subunit, we have examined its effect on the activities of the UL5/52 core enzyme using DNA templates covered by the herpes simplex virus type-1 single-strand DNA- binding protein ICP8. We found that while ICP8 stimulated the DNA helicase activity of the UL5/52 proteins up to 3-fold, maximum stimulation by ICP8 required the presence of UL8 protein. Moreover, UL8 protein was required to reverse the inhibitory effect of ICP8 on the DNA-dependent ATPase and primase activities of the UL5/52 proteins. These observations were specific for ICP8 since the heterologous Escherichia coli singlestrand DNA-binding protein could not substitute for ICP8. These data suggest that UL8 protein mediates an interaction between the UL5/52 core enzyme and ICP8 that optimizes the utilization of ICP8-covered DNA templates during DNA replication.

Original languageEnglish (US)
Pages (from-to)21645-21651
Number of pages7
JournalJournal of Biological Chemistry
Volume271
Issue number35
DOIs
StatePublished - 1996
Externally publishedYes

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DNA Primase
DNA Helicases
DNA-Binding Proteins
Human Herpesvirus 1
Viruses
DNA
Enzymes
Proteins
Genes
DNA Replication
Nucleosides
Escherichia coli
Adenosine Triphosphatases
Human herpesvirus 1 helicase-primase

ASJC Scopus subject areas

  • Biochemistry

Cite this

The UL8 subunit of the herpes simplex virus type-1 DNA helicase-primase optimizes utilization of DNA templates covered by the homologous single- strand DNA-binding protein ICP8. / Gac, Nicolas Tanguy Le; Villani, Giuseppe; Hoffmann, Jean Sébastien; Boehmer, Paul E.

In: Journal of Biological Chemistry, Vol. 271, No. 35, 1996, p. 21645-21651.

Research output: Contribution to journalArticle

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