DNA polymerases α, δ, and ε: Three distinct enzymes from HeLa cells

J. Syvaoja, S. Suomensaari, C. Nishida, J. S. Goldsmith, G. S.J. Chui, S. Jain, S. Linn

Research output: Contribution to journalArticlepeer-review

148 Scopus citations

Abstract

DNA polymerases α, δ, and ε have been purified and characterized from the same HeLa cell extract in order to determine their relationship by comparing them from the same cell type. The catalytic properties and the primary structures of the large subunits of the DNA polymerases as compared by partial peptide mapping with N-chlorosuccinimide are different. Likewise, the small subunit of DNA polymerase ε appears to be distinct from the large subunit of the same polymerase and from the smaller subunits of DNA polymerase α. HeLa DNA polymerase δ is processive only when HeLa proliferating cell nuclear antigen is present, whereas DNA polymerase ε is quite processive in its absence. Inhibitor and activator spectra of DNA polymerases α, δ, and ε also distinguish the three enzymes. These results and immunologic comparisons published elsewhere support the premise that HeLa DNA polymerases α, δ, and ε are distinct enzymes that have common properties with yeast DNA polymerases I, III, and II, respectively.

Original languageEnglish
Pages (from-to)6664-6668
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number17
DOIs
StatePublished - 1990

Keywords

  • mammalian DNA polymerases

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