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

Herpes simplex virus 1 encodes a helicaseprimase 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...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1991-02, Vol.88 (4), p.1105-1109
Hauptverfasser:	Dodson, Mark S., Lehman, I. R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine triphosphatases Adenosine Triphosphatases - genetics Adenosine Triphosphatases - isolation & purification Analytical, structural and metabolic biochemistry Animals Baculoviridae Biological and medical sciences Cell Line Chromatography, Gel Chromatography, Ion Exchange Cytosol - enzymology DNA DNA Helicases DNA Primase Electrophoresis Enzymes Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Gels Genes, Viral GTP Phosphohydrolases - genetics GTP Phosphohydrolases - isolation & purification Human herpesvirus 1 Insect genetics Insect viruses Isomerases Macromolecular Substances Multienzyme Complexes - genetics Multienzyme Complexes - isolation & purification Nucleosides RNA Nucleotidyltransferases - genetics RNA Nucleotidyltransferases - isolation & purification Simplexvirus - enzymology Simplexvirus - genetics
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Beschreibung
Zusammenfassung:	Herpes simplex virus 1 encodes a helicaseprimase 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.
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.88.4.1105