Inhibition of Eukaryotic DNA Polymerase-α by Polydeoxynucleotides

• Published in: Journal of biochemistry (Tokyo) Vol. 92; no. 2; pp. 599 - 602
• Main Authors: OGURO, Mieko, NAGANO, Hiroshi
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.01.1982
• Subjects: Animals; Cells - enzymology; DNA polymerase I; DNA Polymerase II - antagonists & inhibitors; Eukaryotic Cells - enzymology; HeLa Cells; Hemicentrotus pulcherrimus; Humans; Kinetics; Nucleic Acid Synthesis Inhibitors; polydeoxyribonucleotides; Polydeoxyribonucleotides - pharmacology; Pyridoxal Phosphate - pharmacology; Sea Urchins
• ISSN: 0021-924X
• DOI: 10.1093/oxfordjournals.jbchem.a133969

EfFects of polydeoxynucleotides on the activity of DNA polymerase-α from sea urchin embryos were studied. Poly(dG), poly(dC and poly(dC)-oligo(dG)12–18 inhibited DNA polymerase-α activity in the activated DNA-directed reaction but poly(dA), oligo(dT)12–18 and poly(dA)-oligo(dT)12–18 did not inhibit the activity. The inhibitory mode of poly(dC)-oligo(dG)12–18 or poly(dC) was competitive with activated DNA and that of poly(dG) was noncompetitive with activated DNA. Using poly(dA)-oligo(dT)12–18 as a template-primer, the inhibition with either poly(dG) or poly(dC)-oligo(dG)12–18 was competitive with the template-primer. These kinetic results indicate that each of the template-primers tested binds to an identical site on DNA polymerase-α. Similar results were obtained with DNA polymerase-a from HeLa cells.