Characterization of a depurinated-DNA purine-base-insertion activity from Drosophila.
An activity that binds preferentially to depurinated DNA and inserts purines into those sites was partially purified from Drosophila melanogaster embryos. The protein has a sedimentation coefficient of 4.9 S and is devoid of AP (apurinic/apyrimidinic) endonuclease activity. Upon incorporation of purines into apurinic DNA, the number of alkali-labile sites decreases, thus establishing the conversion of depurinated sites into normal nucleotides. The activity requires K+, and is totally inhibited by caffeine or EDTA. Guanine is specifically incorporated into partially depurinated poly(dG-dC) and adenine is specifically incorporated into poly(dA-dT), thus demonstrating the apparent template specificity of the enzyme.
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D000468:Alkalies; D000818:Animals; D001665:Binding Sites; D002110:Caffeine / Q000494:pharmacology; D004247:DNA / Q000235:genetics*; D004260:DNA Repair / Q000187:drug effects; D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D043223:Deoxyribonuclease IV (Phage T4-Induced); D004331:Drosophila melanogaster / Q000235:genetics; D004492:Edetic Acid / Q000494:pharmacology; D004706:Endodeoxyribonucleases / Q000235:genetics*; D011188:Potassium / Q000494:pharmacology; D011687:Purines / Q000378:metabolism
D000468:Alkalies; D011687:Purines; D002110:Caffeine; D004247:DNA; D004492:Edetic Acid; D004706:Endodeoxyribonucleases; D043223:Deoxyribonuclease IV (Phage T4-Induced); D043603:DNA-(Apurinic or Apyrimidinic Site) Lyase; D011188:Potassium