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Nucleic Acids Research, 1992, Vol. 20, No. 18 4699-4703
© 1992

GENOME STRUCTURE AND MAPPING

DNA deoxyribophosphodiesterase of Escherichia coli is associated with exonuclease I

Margarita Sandigursky and William A. Franklin*

Departments of Radiology and Radiation Oncology, Albert Einstein College of Medicine 1300 Morris Park Avenue, Bronx, NY 10461, USA

*To whom correspondence should be addressed

Received August 10, 1992. Accepted August 18, 1992.

DNA deoxyribophosphodiesterase (dRpase) of E.coli catalyzes the release of deoxyrlbose-phosphate moieties following the cleavage of DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease or AP lyase. Exonuclease I is a singlestrand specific DNA nuclease which affects the expression of recombination and repair pathways in E.coli. We show here that a major dRpase activity in E.coli is associated with the exonuclease I protein. Highly purified exonuclease I isolated from an overproducing stain contains high levels of dRpase activity; It catalyzes the release of deoxyribose-5-phosphate from an AP site incised with endonuclease IV of E.coli and the release of 4-hydroxy-2-pentenal-5-phosphate from an AP site incised by the AP lyase activity of endonuclease III of E.coli. A strain containing a deletion of the sbcB gene showed little dRpase activity; the activity could be restored by transformation of the strain with a plasmid containing the sbcB gene. The dRpase activity isolated from an overproducing stain was increased 70-fold as compared to a normal sbcB+ strain (AB3027). These results suggest that the dRpase activity may be important in pathways for both DNA repair and recombination.


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