PMID: 2117830Sep 1, 1990Paper

Aphidicolin-resistant DNA polymerase of bacteriophage phi 29 APHr71 mutant is hypersensitive to phosphonoacetic acid and butylphenyldeoxyguanosine 5'-triphosphate

Virology
K MatsumotoH Hirokawa

Abstract

Bacteriophage phi 29 DNA polymerase is sensitive to aphidicolin (APH). DNA polymerase of the APH-resistant mutant, APHr71, 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 APHr71, indicating that APHr71 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 phi 29 DNA polymerase constitute a structure interacting with deoxynucleotides, pyrophosphate, and APH.

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