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

58 Citations (Scopus)

Abstract

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
Volume89
Issue number20
DOIs
StatePublished - Oct 28 1992

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Exonucleases
DNA-Directed DNA Polymerase
DNA
Oligoribonucleotides
DNA Primers
Oligonucleotides
Glycerol
Thymus Gland
Polyacrylamide Gel Electrophoresis
Peptides

ASJC Scopus subject areas

  • General

Cite this

A 5' to 3' exonuclease functionally interacts with calf DNA polymerase ε. / Siegal, G.; Turchi, J. J.; Myers, T. W.; Bambara, R. A.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 20, 28.10.1992, p. 9377-9381.

Research output: Contribution to journalArticle

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