DNA polymerase-primase from embryos of Drosophila melanogaster. DNA primase subunits

J Biol Chem. 1987 Nov 25;262(33):16105-8.


The primase associated with the DNA polymerase-primase of Drosophila melanogaster fails to show enzymatic turnover. However, it does show turnover when dissociated from the intact polymerase-primase. Both forms of the enzyme can catalyze the synthesis of primers that are not complementary to the DNA template. Like the intact enzyme, the isolated primase synthesizes primers of a unique chain length; however, they are twice as long as those synthesized by the polymerase-primase. The activity of the primase separated from the polymerase-primase is similar in all other respects to the intact polymerase-primase.

Publication types

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

MeSH terms

  • Animals
  • DNA Primase
  • Drosophila melanogaster / embryology
  • Drosophila melanogaster / enzymology*
  • Embryo, Nonmammalian / enzymology
  • Kinetics
  • Macromolecular Substances
  • Molecular Weight
  • RNA Nucleotidyltransferases / isolation & purification*
  • RNA Nucleotidyltransferases / metabolism


  • Macromolecular Substances
  • DNA Primase
  • RNA Nucleotidyltransferases