Use of suppressor analysis to identify DNA polymerase mutations in herpes simplex virus which affect deoxynucleoside triphosphate substrate specificity.
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.
Wang
Y S
YS
Department of Molecular and Cellular Biology, University of Arizona, Tucson 85721.
Woodward
S
S
Hall
J D
JD
D016590:Aphidicolin / Q000494:pharmacology; D004252:DNA Mutational Analysis; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry* / Q000235:genetics; D003854:Deoxyribonucleotides / Q000378:metabolism; D019384:Nucleic Acid Synthesis Inhibitors; D010641:Phenotype; D010746:Phosphonoacetic Acid / Q000494:pharmacology; D018139:Simplexvirus / Q000201:enzymology / Q000235:genetics*; D013379:Substrate Specificity
D003854:Deoxyribonucleotides; D019384:Nucleic Acid Synthesis Inhibitors; D016590:Aphidicolin; D004259:DNA-Directed DNA Polymerase; D010746:Phosphonoacetic Acid