Mitochondrial DNA polymerase from Drosophila melanogaster embryos: kinetics, processivity, and fidelity of DNA polymerization

Biochemistry. 1988 Aug 9;27(16):6046-54. doi: 10.1021/bi00416a033.


The mitochondrial DNA polymerase from embryos of Drosophila melanogaster has been examined with regard to template-primer utilization, processivity, and fidelity of nucleotide polymerization. The enzyme replicates predominantly single-stranded and double-stranded DNAs: the rate of DNA synthesis is greatest on the gapped homopolymeric template poly(dA).oligo(dT), while the highest substrate specificity is observed on single-stranded DNA templates of natural DNA sequence. Kinetic experiments and direct physical analysis of DNA synthetic products indicate that the Drosophila DNA polymerase gamma polymerizes nucleotides by a quasi-processive mechanism. The mitochondrial enzyme demonstrates a high degree of accuracy in nucleotide incorporation which is nearly identical with that of the replicative DNA polymerase alpha from Drosophila embryos. Thus, the catalytic properties of the near-homogeneous Drosophila DNA polymerase gamma are consistent with the in vivo requirements for mitochondrial DNA synthesis as described in a variety of animal systems.

Publication types

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

MeSH terms

  • Animals
  • DNA Polymerase III / metabolism*
  • DNA, Mitochondrial / biosynthesis
  • DNA-Directed DNA Polymerase / metabolism*
  • Drosophila melanogaster / enzymology*
  • Embryo, Nonmammalian / enzymology
  • Kinetics
  • Mitochondria / enzymology*
  • Substrate Specificity


  • DNA, Mitochondrial
  • DNA Polymerase III
  • DNA-Directed DNA Polymerase