Cell
Volume 54, Issue 5, 26 August 1988, Pages 651-658
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Article
Activation of a low specific activity form of DNA polymerase α by inositol-1,4-bisphosphate

https://doi.org/10.1016/S0092-8674(88)80009-6Get rights and content

Summary

A low activity form of DNA polymerase α immunoaffinity-purified from adult-derived human fibroblasts was activated by interaction with phosphatidylinositol-4-monophosphate, while a high activity form of the enzyme did not interact with phosphatidylinositol-4-monophosphate or its derivatives. Phosphatidylinositol-4-monophosphate was apparently hydrolyzed in the presence of a highly purified low activity form of DNA polymerase α, effecting the release of diacylglycerol and the retention of inositol-1,4-bisphosphate by the enzyme complex. The resulting inositol-1,4-bisphosphate/protein complex exhibited increased affinity of binding to DNA template/primer and increased deoxynucleotidyltransferase activity. These data indicate that inositol-1,4-bisphosphate may function as an effector molecule in the activation of a low activity form of human DNA polymerase α and suggest that it may function as a second messenger during the initiation of mitosis in stimulated cells.

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