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

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...

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Bibliographic Details
Published in:Nucleic acids research 1990-06, Vol.18 (12), p.3573-3578
Main Authors: CALDER, J. M, STOW, N. D
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Analytical, structural and metabolic biochemistry
Animals
Baculovirus
Biological and medical sciences
Cells, Cultured
Chromatography
DNA - metabolism
DNA Helicases - metabolism
DNA Primase
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Gene Expression
Genes, Viral
Herpes simplex virus 1
Insecta
Isomerases
Multienzyme Complexes
RNA Nucleotidyltransferases - metabolism
Simplexvirus - enzymology
Simplexvirus - genetics
Spodoptera frugiperda
Viral Proteins - genetics
Viral Proteins - metabolism
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Summary: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.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/18.12.3573