Aphidicolin-resistant DNA polymerase of bacteriophage φ29 APH 71 mutant is hypersensitive to phosphonoacetic acid and butylphenyldeoxyguanosine 5′-triphosphate

Abstract Bacteriophage φ29 DNA polymerase is sensitive to aphidicolin (APH). DNA polymerase of the APH-resistant mutant, APH r 71, was more sensitive to phosphonoacetic acid and butylphenyldeoxyguanosine 5′triphosphate than the wild type. Nucleotide sequence analysis revealed a single transition of G at nucleotide 562 to A in the DNA polymerase gene of APH r 71, indicating that APH r 71 DNA polymerase (572 residues) had a single amino acid substitution from glycine at residue 188 to serine. The results suggest that the site and the neighboring conserved segment of φ29 DNA polymerase constitute a structure interacting with deoxynucleotides, pyrophosphate, and APH.