Human hela cell enzymes that remove phosphoglycolate 3′-end groups from DNA

Thomas A. Winters, Michael Weinfeld, Timothy J. Jorgensen

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2573-2580
Number of pages8
JournalNucleic acids research
Volume20
Issue number10
DOIs
StatePublished - May 25 1992

ASJC Scopus subject areas

  • Genetics

Fingerprint Dive into the research topics of 'Human hela cell enzymes that remove phosphoglycolate 3′-end groups from DNA'. Together they form a unique fingerprint.

Cite this