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.
journal_name
Virologyjournal_title
Virologyauthors
Matsumoto K,Kim CI,Kobayashi H,Kanehiro H,Hirokawa Hdoi
10.1016/0042-6822(90)90416-osubject
Has Abstractpub_date
1990-09-01 00:00:00pages
337-9issue
1eissn
0042-6822issn
1096-0341journal_volume
178pub_type
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