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PMID: 2163521 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities.

Nucleic acids research ·Vol. 18 ·No. 12 ·1990-06-25 ·Pages 3573-8

Calder JM, Stow ND

Abstract

The herpes simplex virus type 1 helicase-primase complex consists of the products of the UL5, UL8 and UL52 genes. We have expressed these proteins in insect cells using baculovirus vectors and studied the requirements for enzymatic activities associated with the DNA unwinding function of the complex. In agreement with a recent report (Dodson, M.S., Crute, J.J., Bruckner, R.C. and Lehman, I.R. 1989, J. Biol. Chem. 264, 20835-20838) we find that DNA-dependent ATPase and DNA helicase activities are assembled in vivo in insect cells triply infected with viruses expressing the UL5, UL8 and UL52 proteins. Moreover, these activities were also detected in cells in which only the UL5 and UL52 products were expressed indicating that the presence of the UL8 protein is essential for neither the ATPase nor helicase activity of the complex.

MeSH Terms
Adenosine Triphosphatases/metabolism Animals Cells, Cultured Chromatography DNA/metabolism DNA Helicases/metabolism DNA Primase Gene Expression Genes, Viral Insecta Multienzyme Complexes RNA Nucleotidyltransferases/metabolism Simplexvirus/enzymology,genetics Viral Proteins/genetics,metabolism
Chemicals
Multienzyme Complexes Viral Proteins DNA DNA Primase RNA Nucleotidyltransferases helicase-primase, Human herpesvirus 1 Adenosine Triphosphatases DNA Helicases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Calder J M
Medical Research Council Virology Unit, Institute of Virology, Glasgow, UK.
Stow N D
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35 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/18.12.3573
Published
1990-06-25
Pages
3573-8
Language
English
Region
England
NLM ID
0411011
PMCID
PMC331012
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/18.12.3573 PMC Full Text View journal details
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