TY - JOUR
T1 - Human hela cell enzymes that remove phosphoglycolate 3′-end groups from DNA
AU - Winters, Thomas A.
AU - Weinfeld, Michael
AU - Jorgensen, Timothy J.
N1 - Funding Information:
The authors thank Pamela S.Russell for technical assistance and Sandra Hawkins for secretarial assistance. This work was supported by Grant CA 48716 (to T.J.J.) from the National Cancer Institute, National Institutes of Health, U.S. DHHS, and a grant (to M.W.) from the Research Initiative Program of the Alberta Cancer Board.
PY - 1992/5/25
Y1 - 1992/5/25
N2 - 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.
AB - 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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U2 - 10.1093/nar/20.10.2573
DO - 10.1093/nar/20.10.2573
M3 - Article
C2 - 1375993
AN - SCOPUS:0026554433
VL - 20
SP - 2573
EP - 2580
JO - Nucleic Acids Research
JF - Nucleic Acids Research
SN - 1362-4962
IS - 10
ER -