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. 1992 Oct 15;89(20):9377-81.
doi: 10.1073/pnas.89.20.9377.

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

G Siegal  1 , J J Turchi, T W Myers, R A Bambara
Affiliations

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

G Siegal et al. Proc Natl Acad Sci U S A. .

Abstract

Analysis of fractions containing purified DNA polymerase epsilon 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 alpha and delta on exonuclease activity are also observed but with differences in the pattern of products.

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