Abstract

A protein factor having exonucleolytic activity on bleomycin-damaged DNA and providing priming sites for DNA polymerases existed in a DNA polymerase beta fraction partially purified by ion exchange chromatography from an extract of permeable mouse ascites sarcoma (SR-C3H/He) cells. The exonuclease was separated from DNA polymerase beta by single-stranded DNA-cellulose chromatography, and partially characterized. The enzyme is suggested to be involved in the initial step of repair of bleomycin-damaged DNA in removing 3' ends (3'-phosphoglycolate termini) of bleomycin-damaged DNA.

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