Cotterill, S., Chui, G., Lehman, I.R. (1987). DNA polymerase-primase from embryos of Drosophila melanogaster. The DNA polymerase subunit. J. Biol. Chem. 262(33): 16100--16104.
FlyBase ID
FBrf0046590
Publication Type
Research paper
Abstract
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.
