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Nucleic Acids Research, 1992, Vol. 20, No. 10 2573-2580
© 1992

ENZYMOLOGY

Human HeLa cell enzymes that remove phosphoglycolate 3'-end groups from DNA

Thomas A. Winters, Michael Weinfeld1 and Timothy J. Jorgensen*

Department of Radiation Medicine, Vincent T.Lombardi Cancer Research Center, Georgetown University Medical Center 3800 Reservoir Road NW, Washington DC 20007, USA 1Radiobiology Program, Cross Cancer Institue 11560 University Avenue, Edmonton, Alberta T6G 1Z2, Canada

* To whom correspondence should be addressed

Received December 2, 1991. Revised April 7, 1992. Accepted April 7, 1992.

We have purified three chromatographically distinct human enzyme activities from HeLa cells, that are capable of converting bleomycin-treated DNA into a substrate for E. coli DNA polymerase I. The bleomycin-treated DNA substrate used in this study has been characterized via a 32P-postiabeling assay and shown to contain strand breaks with 3'-phosphoglycolate termini as greater than 95% of the detectable dose-dependent lesions. The purified HeLa cell enzymes were shown to be capable of removing 3'-phosphoglycolates from this substrate. Also 3'-phosphoglycolate removal and nucleotide incorporation were enzyme have been determined to possess Class II AP endonuclease activity. The enzymes lack 3' – 5' exonuclease activity and are, therefore, dissimilar to exonuclease III—an E. coli enzyme that can remove 3'-phosphoglycolate.


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