Comparative study of DNA polymerases α and β from sea urchin embryos
DOI:
https://doi.org/10.7124/bc.000189Abstract
Two DNA polymerases were isolated from embryonic cells of the sea urchin Strongylocentrotus mermedlus. In terms of physicochemical properties and primer-template specificity these enzymes are classified as DNA polymerases α and β. DNA polymerase a can interact both with single strand and 3'-hydroxyl termini in gapped DNA. The interaction of DNA polymerase α with single-stranded sites depends on the template base composition. DNA polymerase p recognizes only 3' primer termini (hydroxyl or phosphoryl). DNA polymerase a realizes DNA synthesis via a moderately processive mechanism and is unable to fill gaps in the DNA chain to completion. In contrast, DNA polymerase β is a distributive enzyme and fills gaps in the DNA chain completely.References
Weissbach A. Eukaryotic DNA polymerases. Annu Rev Biochem. 1977;46:25-47.
De Petrocellis B, Parisi E, Filosa S, Capasso A. Separation and partial characterization of DNA polymerases in sea urchin Paracentrotus lividus eggs. Biochem Biophys Res Commun. 1976;68(3):954-60.
Racine FM, Morris PW. DNA polymerase alpha and beta in the California urchin. Nucleic Acids Res. 1978;5(10):3945-57.
Loeb LA. Purification and properties of deoxyribonucleic acid polymerase from nuclei of sea urchin embryos. J Biol Chem. 1969;244(7):1672-81.
Suzuki-Hori C, Nagano H, Mano Y. DNA polymerase-beta from the nuclear fraction of sea urchin embryos: characterization of the purified enzyme. J Biochem. 1977;82(6):1613-21.
Hobart PM, Infante AA. A low molecular weight DNA polymerase beta in the sea urchin Strongylocentrotus purpurantus. Partial purification, properties, and changes in development. J Biol Chem. 1978;253(22):8229-38.
Terent'ev LL, Terent'eva NA, Rassazov VA. DNA-polymerase from sea urchin (Strongylocentrotus intermedius. Embryos. Biokhimiia. 1980;45(9):1603-8.
Terent'ev LL, Terent'eva NA, Rasskazov VA. Processing and some properties of DNA-polymerase alpha from sea urchin embryos. Biokhimiia. 1983;48(2):224-9.
Terent'ev LL, Terent'eva NA, Rasskazov VA. Isolation and various properties of beta DNA polymerase from the embryos of the sea urchin Strongylocentrotus intermedius. Biokhimiia. 1984;49(7):1103-9.
Terent'ev LA, Terentyeva HA, Rasskazov VA. Comparative studies of DNA polymerases ? and ? of sea urchin embryos. In the book.: Structure and function of the cell nucleus: Proc. of reports. Proc. symposium. Pushchino, 1984, p. 278-279.
Wang TS, Sedwick WD, Korn D. Nuclear deoxyribonucleic acid polymerase. Further observations on the structure and properties of the enzyme from human KB cells. J Biol Chem. 1975;250(17):7040-4.
Bollum FJ. Mammalian DNA polymerases. Prog Nucleic Acid Res Mol Biol. 1975;15(0):109-44.
Romberg A. DNA replication. Ed. W. H. Freeman. San Francisco : Stanford Univ., 1980. 380 p.
Korn D, Fisher PA, Wang TS. Mechanisms of catalysis of human DNA polymerases alpha and beta. Prog Nucleic Acid Res Mol Biol. 1981;26:63-81.
Das SK, Fujimura RK. Processiveness of DNA polymerases. A comparative study using a simple procedure. J Biol Chem. 1979;254(4):1227-32.
Bambara RA, Uyemura D, Choi T. On the processive mechanism of Escherichia coli DNA polymerase I. Quantitative assessment of processivity. J Biol Chem. 1978;253(2):413-23.
Fisher PA, Wang TS, Korn D. Enzymological characterization of DNA polymerase alpha. Basic catalytic properties processivity, and gap utilization of the homogeneous enzyme from human KB cells. J Biol Chem. 1979;254(13):6128-37.
