Open AccessDoes butyiphenyl-deoxyguanosine triphosphate differentially inhibit DNA polymerase α and δ activities in permeabilized HeLa cells?
Author(s) -
Aimee L. Jackson
Publication year - 1990
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/18.4.753
Subject(s) - biology , dna polymerase , okazaki fragments , dna polymerase ii , aphidicolin , dna clamp , dna replication , dna polymerase i , polymerase , dna polymerase delta , microbiology and biotechnology , dna synthesis , biochemistry , dna , primase , eukaryotic dna replication , polymerase chain reaction , gene , reverse transcriptase
In eukaryotic cells, two enzymes, DNA polymerases alpha and delta, are thought to play major roles in DNA synthesis. I have used butylphenyl dGTP (BuPdGTP), a potent inhibitor of purified DNA polymerase alpha, to assess the relative activities of these enzymes in two permeabilized cell systems. In both instances BuPdGTP eliminated all of the activity which was sensitive to aphidicolin. However, no conditions were found where BuPdGTP preferentially inhibited the synthesis of Okazaki fragments--the presumed products of DNA polymerase alpha activity. This implies that DNA polymerase activities on the two sides of the replication fork are unable to operate independently, being just two elements of the integrated replication machinery that undertakes DNA synthesis in permeabilized cells.