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Results for “Exonucleases”

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PubMed1984

Novel interaction of aphidicolin with herpes simplex virus DNA polymerase and polymerase-associated exonuclease.

DNA polymerases induced by herpes simplex virus (HSV)-1 (KOS) and by three phosphonoformic acid-resistant strains were purified and the interaction of these enzymes with aphidicolin was examined. Incorporation of dATP, dCTP, and dTTP into activated DNA by parental enzyme was inhibited competitively by aphidicolin whereas dGTP incorporation was inhibited noncompetitively. Phosphonoformic acid-resistant enzymes were altered in KM and KI values for substrate and inhibitor, and two were inhibited by aphidicolin via the same modes as parental enzyme. However, aphidicolin competitively inhibited incorporation of dGTP by the third phosphonoformic acid-resistant enzyme under identical assay conditions. Two phosphonoformic acid-resistant enzymes were more sensitive than parental enzyme to inhibition by aphidicolin, indicating a close association between binding determinants for aphidicolin and for phosphonoformic acid on the virus DNA polymerase molecule. Aphidicolin inhibited hydrolysis of polynucleotide by HSV-1 DNA polymerase-associated nuclease. Inhibition was uncompetitive with DNA and the KI value (0.09 microM) was within the range of those calculated during nucleotide incorporation (0.071-0.74 microM). Therefore, aphidicolin may produce antiviral effects both by inhibition of deoxynucleotide incorporation and by deleterious effects resulting from inhibition of polymerase-associated nuclease.

Animals↗
PubMed1981

Lambda exonuclease.

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Bacteriophage lambda↗
PubMed1993

Effect of a template-located 2',2'-difluorodeoxycytidine on the kinetics and fidelity of base insertion by Klenow (3'-->5'exonuclease-) fragment.

Gemcitabine [2',2'-difluorodeoxycytidine (dFdCyd)], a potent antitumor agent, inhibits DNA synthesis and is incorporated internally into DNA. The effect of a template-incorporated dFdCyd molecule (dFdCyd-) on DNA polymerase function was examined. Two 25-base deoxyoligonucleotides were synthesized with either a single dFdCyd- or template-incorporated deoxycytidine molecule (dCyd-) at the same position. Each was annealed separately to an identical complementary 5'-32P-labeled primer and extended by the Klenow fragment (3'-->5' exo-) of DNA polymerase I. "Correct" insertion of dGMP was 80-fold less efficient opposite dFdCyd- than dCyd-. A comparison of misinsertion efficiencies opposite template dFdCyd gave values of 2.7 x 10(-2) for dAMP insertion, 1.1 x 10(-3) for dTMP insertion, and 5.9 x 10(-4) for dCMP insertion. A similar measurement opposite template dC gave values of 1.8 x 10(-4), 1.7 x 10(-4), and 2.9 x 10(-6) for dAMP, dTMP, and dCMP insertion, respectively. Thus, the presence of dFdCyd on the template strand inhibited "normal" DNA synthesis and increased deoxyribonucleotide misinsertion frequencies. Pausing during DNA synthesis occurred directly opposite template dFdCyd suggesting that dFdC.dG base pairs might be less stable than normal dC.dG pairs, resulting in a decreased rate of primer extension beyond this site. Consistent with kinetic data, thermal denaturation measurements using comparable surrounding sequences showed that dFdC.dG "correct" pairs were less stable than dC.dG base pairs. Measurements on base mispairs showed that dFdC.dC was more stable than dC.dC, while no measurable Tm differences were found between polymers containing dFdC.dA and dC.dA or dFdC.dT, and dC.dT.

Antimetabolites, Antineoplastic↗