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

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

Virology

journal_title

Virology

authors

Matsumoto K,Kim CI,Kobayashi H,Kanehiro H,Hirokawa H

doi

10.1016/0042-6822(90)90416-o

subject

Has Abstract

pub_date

1990-09-01 00:00:00

pages

337-9

issue

1

eissn

0042-6822

issn

1096-0341

journal_volume

178

pub_type

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