Interaction of phosphatidylinositol-4-monophosphate with a low activity form of dna polymerase alpha: a potential mechanism for enzyme activation

V. L. Sylvia, C. O. Joe, J. O. Norman, G. M. Curtim, R. D. Tilley, D. L. Busbee

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

1. 1. DNA polymerase alpha isolated from Norman murine myxosarcoma exhibited two isozyme forms, one with low specific activity and low DNA binding affinity (a1), and one with high specific activity and high DNA binding affinity (A2). 2. 2. DNA polymerase alpha a1, but not A2, showed a significant increase in specific activity after treatment with phosphatidylinositol, ATP and phosphatidylinositol kinase, or with phosphatidylinositol-4-monophosphate. 3. 3. Treatment of DNA polymerase alpha a1 with the phospholipase C hydrolysis product of phosphatidylinositol-4-monophosphate, inositol-1,4-bisphosphate, was sufficient to effect the transient increase in activity of polymerase a1 to a form not chromatographically distinguishable from isozyme form A2.

Original languageEnglish (US)
Pages (from-to)347-353
Number of pages7
JournalInternational Journal of Biochemistry
Volume21
Issue number4
DOIs
StatePublished - 1989
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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