Purification and characterization of varicella-zoster virus-induced DNA polymerase

J Virol. 1978 May;26(2):249-56. doi: 10.1128/JVI.26.2.249-256.1978.


Infection of WI-38 human fibroblasts with varicella-zoster virus led to the stimulation of host cell DNA polymerase synthesis and induction of a new virus-specific DNA polymerase. This virus-induced DNA polymerase was partially purified and separated from host cell enzymes by DEAE-cellulose and phosphocellulose column chromatographies. This virus-induced enzyme could be distinguished from host cell enzyme by its chromatographic behavior, template specificity, and its requirement of salt for maximal activity. The enzyme could efficiently use poly(dC).oligo(dG)12-18 as well as poly(dA).oligo(dT)12-18 as template-primers. It required Mg2+ for maximal polymerization activity and was sensitive to phosphonoacetic acid, to which host alpha- and beta-DNA polymerase were relatively resistant. In addition, this induced DNA polymerase activity was enhanced by adding 60 mM (NH4)2SO4 to the reaction mixture.

Publication types

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

MeSH terms

  • Ammonium Sulfate / pharmacology
  • Cell Line
  • DNA-Directed DNA Polymerase / isolation & purification
  • DNA-Directed DNA Polymerase / metabolism*
  • Enzyme Induction
  • Herpesvirus 3, Human / enzymology*
  • Hydroxymercuribenzoates / pharmacology
  • Magnesium / pharmacology
  • Phenanthrolines / pharmacology
  • Phosphonoacetic Acid / pharmacology
  • Polydeoxyribonucleotides / metabolism


  • Hydroxymercuribenzoates
  • Phenanthrolines
  • Polydeoxyribonucleotides
  • DNA-Directed DNA Polymerase
  • Magnesium
  • Phosphonoacetic Acid
  • Ammonium Sulfate