A 5' to 3' exonuclease functionally interacts with calf DNA polymerase ε

G. Siegal, J. J. Turchi, T. W. Myers, R. A. Bambara

Research output: Contribution to journalArticle

59 Scopus citations


Analysis of fractions containing purified DNA polymerase ε from calf thymus has revealed the presence of a 5' to 3' exonuclease activity that is specific for a single strand of duplex DNA. This activity is capable of degrading a 3'-labeled oligonucleotide hybridized to M13mp18 DNA. When a second oligonucleotide primer is annealed 3 bases upstream, degradation of the downstream primer is strictly dependent on DNA synthesis from the upstream primer. Replacement of the downstream primer by an oligoribonucleotide of identical sequence results in a similar pattern of exonucleolytic activity. The activity has been highly purified and found to cosediment in glycerol gradients with a peptide of 56 kDa as judged by SDS/PAGE analysis. Effects of calf DNA polymerase α and δ on exonuclease activity are also observed but with differences in the pattern of products.

Original languageEnglish (US)
Pages (from-to)9377-9381
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number20
StatePublished - 1992

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'A 5' to 3' exonuclease functionally interacts with calf DNA polymerase ε'. Together they form a unique fingerprint.

  • Cite this