Abstract
We identified a DNA polymerase species inDrosophila melanogasterembryos, and purified it. This polymerase shared some common properties with DNA polymerase ϵ from mammals and yeast as follows; it has a preference for poly(dA)/oligo(dT) as a template/primer, it is highly processive in DNA synthesis, it co-fractionates with 3′-5′ exonuclease activity, it is sensitive to aphidicolin and is resistance to ddTTP. The polymerase activity was inhibited in the immuno-precipitation assay with anti-pol-ϵ antibodies, which were produced against a polypeptide coded on the cDNA of a putativeDrosophilapol-ϵ we isolated previously. Using these antibodies, Western blot analysis revealed that this polymerase is a 250kDa polypeptide, which is the same size as observed in mammals and yeast. These results indicate thatDrosophilaproduces the ϵ-class of DNA polymerase, and like mammals or yeast, possesses the 5 typical classes of DNA polymerases (α to ϵ) in its embryos.
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