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DNA polymerase-primase from embryos of Drosophila melanogaster. DNA primase subunits
S Cotterill1, G Chui, I R Lehman
1Department of Biochemistry, Stanford University School of Medicine, California 94305.
The Journal of Biological Chemistry
|November 25, 1987
Abstract:
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.