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Nucleic Acids Research, 1979, Vol. 6, No. 5 1881-1894
© 1979

Articles

The effect of antibiotics on the T4 polynucleotide ligase catalyzed template dependent polymerization of oligodeoxythymidylates

Bernd W. Kalisch and Johan H. van de Sande

Division of Medical Bicshemistry, Faculty of Medicine, University of Calgary Calgary, Alberta, T2N 1 N4, Canada

Received January 15, 1979. The poly(dA) dependent T4 polynucleotide ligase catalyzed polymerization of oligodeoxythymidylates is dependent upon duplex stability. The antibiotics ethidium bromide, netropsin and Hoechst 33258 stabilize the duplex poly(dA). p(dT)n (n=6–10) to thermal denaturation. Ethidium bromide to DNA ratio of 1.25 and netropsin or Hoechst 33258 to DNA ratio of 0.1 the Tm of d(pT)10 poly (dA) was increased by 10° and 25°C respectively. The T4 polynucleotide ligase activity was not inhibited under these conditions and temperature optimum of joining of d(pT)10 poly(dA) was increased 5° to 10° by the binding of the antibiotics. Duplexes containing shorter oligodeoxythymidylates required lower concentrations of the antibiotics netropsin or Hoechst 33258 to show no inhibition of T4 polynucleotide ligase. The temperature optima of joining the duplexes d(pT)6 poly(dA) and d(PT)8 poly (dA) were increased by 5°C upon binding of the antibiotics. Polyacrylamide gel analysis of the T4 polynucleotide ligase catalyzed joining of the oligodeoxythymidylates showed that the presence of antibiotics affected the product distribution of the polymerized oligomers.


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