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. 1985 Nov 15;232(1):285-8.
doi: 10.1042/bj2320285.

Characterization of a depurinated-DNA purine-base-insertion activity from Drosophila

W A Deutsch, A L Spiering

Characterization of a depurinated-DNA purine-base-insertion activity from Drosophila

W A Deutsch et al. Biochem J. .

Abstract

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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