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J. Biol. Chem., Vol. 262, Issue 33, 16100-16104, 11, 1987

DNA polymerase-primase from embryos of Drosophila melanogaster. The DNA polymerase subunit

S Cotterill, G Chui and IR Lehman
Department of Biochemistry, Stanford University School of Medicine, California 94305.

The DNA polymerase-primase from Drosophila melanogaster has been separated into its constituent polymerase and primase subunits by sedimentation in glycerol gradients containing 50% ethylene glycol. Both activities have been obtained in good yield. The properties of the 182-kDa polymerase subunit are similar to those of the intact four- subunit enzyme. However, there are three significant differences. (i) The polymerase activity of the 182-kDa subunit shows an increased thermolability; (ii) the pause sites during replication of singly primed, single-stranded circular DNA by the 182-kDa subunit are altered; and (iii) unlike the intact enzyme, the 182-kDa subunit is highly processive in the presence of the single-stranded DNA-binding protein of Escherichia coli.
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