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The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicase-primase is required for the unwinding of single strand DNA-binding protein (ICP8)-coated DNA substrates.

Journal article
Authors Maria Falkenberg
D A Bushnell
Per Elias
I R Lehman
Published in The Journal of biological chemistry
Volume 272
Issue 36
Pages 22766-70
ISSN 0021-9258
Publication year 1997
Published at Institute of Medical Biochemistry
Pages 22766-70
Language en
Links www.ncbi.nlm.nih.gov/entrez/query.f...
Keywords Animals, Cell Line, DNA Helicases, metabolism, DNA Primase, DNA-Binding Proteins, Enzyme Activation, Herpesvirus 1, Human, metabolism, Protein Conformation, Refractometry, Spodoptera, Substrate Specificity, Surface Properties, Viral Proteins, chemistry, metabolism
Subject categories Chemistry

Abstract

The Herpes simplex virus type 1 primosome consists of three subunits that are the products of the UL5, UL8, and UL52 genes. The heterotrimeric enzyme has DNA-dependent ATPase, helicase, and primase activities. Earlier studies show that a subassembly consisting of the UL5 and UL52 gene products was indistinguishable from the heterotrimeric enzyme in its helicase and primase activities. We demonstrate here that the UL8 protein is required for the helicase activity of the UL5/52 subassembly on long duplex DNA substrates (>30 nucleotides) with a single-stranded DNA loading site fully coated with the virus-encoded single strand DNA binding protein, ICP8. The Escherichia coli single strand DNA binding protein cannot substitute for ICP8, suggesting a specific physical interaction between ICP8 and the UL8 protein. Surface plasmon resonance measurements demonstrated an interaction between ICP8 and the UL5/52/8 heterotrimer but not with the UL5/52 subassembly or the UL8 protein alone. At a subsaturating level of ICP8, the UL5/52 subassembly does show helicase activity, suggesting that the subassembly can bind to single-stranded DNA but not to ICP8-coated DNA.

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