Purification and characterization of bacteriophage N4-induced DNA polymerase.

作者: G K Lindberg , J K Rist , T A Kunkel , A Sugino , L B Rothman-Denes

DOI: 10.1016/S0021-9258(18)37961-4

关键词:

摘要: Coliphage N4 replication is independent of most host DNA functions except for the 5'----3' exonuclease activity polA, ligase, gyrase, and ribonucleotide reductase (Guinta, D., Stambouly, J., Falco, S. C., Rist, J. K., Rothman-Denes, L. B. (1986) Virology 150, 33-44). It therefore expected that codes required its genome. In this paper we report purification N4-coded polymerase from N4-infected cell extracts by following on a gapped template in an vitro complementation system (Rist, Pearle, M., Sugino, A., Biol. Chem. 261, 10506-10510). The enzyme composed one polypeptide, Mr 87,000. active templates containing short gaps synthesizing with high fidelity quasi-processive manner. A strong 3'----5' associated polypeptide. No or strand-displacing activities were detected.

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