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Inhibition of RNA-dependent DNA polymerase by thymidylate derivatives.

The effects of several thymidylate derivatives with reactive substituents on the RNA-dependent DNA polymerase of Rauscher murine leukemia virus were investigated. The reactive substituents include haloacetamido groups potentially capable of forming covalent bonds with the enzyme. The kinetics of inhibition with thymidine-3′,5′-di- m -bromoacetamidophenyl phosphate, the most active agent of the series, was competitive with poly(rA)·oligo(dT), the model primer-template used, and noncompetitive with the deoxynucleoside triphosphates. Preincubation of the virus with thymidine-3′,5′-di- m -bromoacetamidophenyl phosphate magnified the inhibition of DNA synthesis.

Inhibition of the reactions directed by DNA templates, such as salmon sperm DNA and poly[d(A-T)], was comparable to that found with poly(rA)·oligo(dT). The inhibition of tumor virus DNA polymerase is not selective, since we observed comparable inhibition of a DNA-dependent DNA-polymerase partly purified from phytohemagglutinin-stimulated normal human blood lymphocytes.