Association of DNA primase with the beta/gamma subunits of DNA polymerase alpha from Drosophila melanogaster embryos

J Biol Chem. 1983 Aug 10;258(15):9037-9.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Centrifugation, Density Gradient
  • DNA Polymerase II / metabolism*
  • DNA Primase
  • DNA-Directed DNA Polymerase / metabolism*
  • Drosophila melanogaster / embryology*
  • Drosophila melanogaster / enzymology
  • Electrophoresis, Polyacrylamide Gel
  • Macromolecular Substances
  • RNA Nucleotidyltransferases / metabolism*

Substances

  • Macromolecular Substances
  • DNA Polymerase II
  • DNA Primase
  • RNA Nucleotidyltransferases
  • DNA-Directed DNA Polymerase