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. 1988 Nov;7(11):3617-22.
doi: 10.1002/j.1460-2075.1988.tb03240.x.

DNA deoxyribophosphodiesterase

W A Franklin  1 , T Lindahl
Affiliations

DNA deoxyribophosphodiesterase

W A Franklin et al. EMBO J. 1988 Nov.

Abstract

A previously unrecognized enzyme acting on damaged termini in DNA is present in Escherichia coli. The enzyme catalyses the hydrolytic release of 2-deoxyribose-5-phosphate from single-strand interruptions in DNA with a base-free residue on the 5' side. The partly purified protein appears to be free from endonuclease activity for apurinic/apyrimidinic sites, exonuclease activity and DNA 5'-phosphatase activity. The enzyme has a mol. wt of approximately 50,000-55,000 and has been termed DNA deoxyribophosphodiesterase (dRpase). The protein presumably is active in DNA excision repair to remove a sugar-phosphate residue from an endonucleolytically incised apurinic/apyrimidinic site, prior to gap filling and ligation.

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References

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