Association of DNA primase with the beta/gamma subunits of DNA polymerase alpha from Drosophila melanogaster embryos.
The DNA polymerase and primase activities of the intact DNA polymerase alpha from early embryos of Drosophila melanogaster co-sediment in native glycerol gradients. However, the activities are separated in glycerol gradients containing 2.8 M urea after treatment of the enzyme with 3.4 M urea. The 182,000-dalton alpha subunit which is required for DNA polymerase activity (Kaguni, L.S., Rossignol, J.-M., Conaway, R. C., and Lehman, I.R. (1983) Proc. Natl. Acad. Sci. U. S.A. 80, 2221-2225) is not required for DNA primase activity. Instead, primase activity resides in the 60,000-dalton (beta) and/or the 50,000-dalton (gamma) subunit. Neither polymerase nor primase has been found in association with the 73,000-dalton polypeptide which co-purifies with the intact enzyme.
D000818:Animals; D002499:Centrifugation, Density Gradient; D004257:DNA Polymerase II / Q000378:metabolism*; D019915:DNA Primase; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000196:embryology* / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D012316:RNA Nucleotidyltransferases / Q000378:metabolism*
D046911:Macromolecular Substances; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases; D004257:DNA Polymerase II; D004259:DNA-Directed DNA Polymerase