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. 1978 Jul;5(7):2565–2575. doi: 10.1093/nar/5.7.2565

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

Christine L Brakel 1, Alan B Blumenthal 1
PMCID: PMC342186  PMID: 97638

Abstract

The activity of a 7.3S-8.3S Drosophila DNA polymerase was characterized in detail using poly dA·p(dT)[unk] and poly rA·p(dT)[unk]. With poly dA·p(dT)[unk], Mg2+ ion was the preferred divalent cation, and enzyme activity was inhibited by K+ ion and by spermidine. With poly rA·p(dT)[unk], 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 dA·p(dT)[unk] was more stable to thermal inactivation than was enzyme activity with poly rA·p(dT)[unk]. 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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