Use of suppressor analysis to identify DNA polymerase mutations in herpes simplex virus which affect deoxynucleoside triphosphate substrate specificity

J Virol. 1992 Mar;66(3):1814-6. doi: 10.1128/JVI.66.3.1814-1816.1992.

Abstract

Herpes simplex virus DNA polymerase mutations which map in the N-terminal part of the protein and appear to alter deoxynucleoside triphosphate (dNTP) substrate specificity are described. These mutations suppress a drug hypersensitivity associated with the downstream mutation, Aphr10. We suggest that the mutant residues form part of the dNTP-binding site, a site previously thought to be confined to the C terminus.

Publication types

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

MeSH terms

  • Aphidicolin / pharmacology
  • DNA Mutational Analysis
  • DNA-Directed DNA Polymerase / chemistry*
  • DNA-Directed DNA Polymerase / genetics
  • Deoxyribonucleotides / metabolism
  • Nucleic Acid Synthesis Inhibitors
  • Phenotype
  • Phosphonoacetic Acid / pharmacology
  • Simplexvirus / enzymology
  • Simplexvirus / genetics*
  • Substrate Specificity

Substances

  • Deoxyribonucleotides
  • Nucleic Acid Synthesis Inhibitors
  • Aphidicolin
  • DNA-Directed DNA Polymerase
  • Phosphonoacetic Acid