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Nucleic Acids Research, 1978, Vol. 5, No. 7 2565-2575
© 1978

Articles

Replication of poiy dA and poly rA by a Drosophila DNA polymerase

Christine L. Brakel and Alan B. Blumenthal

Laboratory of Radiobiology, University of California San Francisco, CA 94143, USA

Received April 10, 1978. The activity of a 7.3S–8.3S Drosophila DNA polymerase was characterized in detail using poly Formula and poly Formula With poly Formula Mg2+ ion was the preferred divalent cation, and enzyme activity was inhibited by K+ ion and by spermidine. With poly Formula, Mn2+ ion was the preferred divalent cation and enzyme activity was stimulated by K+ ion and by spermidine. The dependence of enzyme activity on the concentration of primer-template and on the ratio of primer to template was the same in both reactions. The two enzyme activities were identically inhibited by N-ethylmaleimide. Poly dA was replicated extensively and poly rA was replicated partially. The activation energy for poly dA replication was twice that for poly rA replication. Enzyme activity with poly Formula was more stable to thermal inactivation than was enzyme activity with poly Formula. These studies suggest that the same enzyme responds to both the deoxy- and the ribohomopolymer template but that the mechanisms of replication may be different.


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