The herpes simplex virus 1 origin binding protein: a DNA helicase

J Biol Chem. 1991 Feb 5;266(4):2669-74.

Abstract

A recombinant herpes simplex 1 origin binding protein, the product of the herpes UL9 gene, has been overexpressed in mammalian cells and purified to near homogeneity. The origin binding protein shows DNA-dependent nucleoside 5'-triphosphatase and DNA helicase activities in addition to its origin binding activity. The ability to hydrolyze nucleoside 5'-triphosphates is influenced strongly by the structure and sequence of the DNA cofactor. The properties of the recombinant origin binding protein are identical to those of the protein synthesized in herpes simplex 1-infected mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Animals
  • Base Sequence
  • Cattle
  • Cells, Cultured
  • Chromatography, Gel
  • Cloning, Molecular
  • DNA Helicases / genetics*
  • DNA Helicases / isolation & purification
  • DNA Helicases / metabolism
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / isolation & purification
  • DNA-Binding Proteins / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Gene Expression
  • Genes, Viral
  • Molecular Sequence Data
  • Simplexvirus / enzymology
  • Simplexvirus / genetics*
  • Substrate Specificity
  • Viral Proteins / genetics*
  • Viral Proteins / isolation & purification
  • Viral Proteins / metabolism

Substances

  • DNA-Binding Proteins
  • Viral Proteins
  • origin-binding proteins, viral
  • Adenosine Triphosphatases
  • DNA Helicases