Inhibition of eukaryotic DNA polymerase-alpha by polydeoxynucleotides.
Effects of polydeoxynucleotides on the activity of DNA polymerase-alpha from sea urchin embryos were studied. Poly(dG), poly(dC) and poly(dC)-oligo(dG)12-18 inhibited DNA polymerase-alpha 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-alpha. Similar results were obtained with DNA polymerase-alpha from HeLa cells.
D000818:Animals; D002477:Cells / Q000201:enzymology*; D004257:DNA Polymerase II / Q000037:antagonists & inhibitors*; D005057:Eukaryotic Cells / Q000201:enzymology*; D006367:HeLa Cells; D006801:Humans; D007700:Kinetics; D019384:Nucleic Acid Synthesis Inhibitors; D011089:Polydeoxyribonucleotides / Q000494:pharmacology*; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D012617:Sea Urchins
D019384:Nucleic Acid Synthesis Inhibitors; D011089:Polydeoxyribonucleotides; D011732:Pyridoxal Phosphate; D004257:DNA Polymerase II