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Activation of mammalian DNA ligase I through phosphorylation by casein kinase II.

Abstract : Mammalian DNA ligase I has been shown to be a phosphoprotein. Dephosphorylation of purified DNA ligase I causes inactivation, an effect dependent on the presence of the N-terminal region of the protein. Expression of full-length human DNA ligase I in Escherichia coli yielded soluble but catalytically inactive enzyme whereas an N-terminally truncated form expressed activity. Incubation of the full-length preparation from E. coli with purified casein kinase II (CKII) resulted in phosphorylation of the N-terminal region and was accompanied by activation of the DNA ligase. Of a variety of purified protein kinases tested, only CKII stimulated the activity of calf thymus DNA ligase I. Tryptic phosphopeptide analysis of DNA ligase I revealed that CKII specifically phosphorylated a major peptide also apparently phosphorylated in cells, implying that CKII is a protein kinase acting on DNA ligase I in the cell nucleus. These data suggest that DNA ligase I is negatively regulated by its N-terminal region and that this inhibition can be relieved by post-translational modification.
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Contributor : Claude Prigent Connect in order to contact the contributor
Submitted on : Wednesday, March 26, 2014 - 8:23:22 AM
Last modification on : Thursday, January 13, 2022 - 2:20:34 PM


  • HAL Id : inserm-00966023, version 1
  • PUBMED : 1639065



Claude Prigent, Dana D. Lasko, Ken-Ichi Kodama, James R. Woodgett, Tomas Lindahl. Activation of mammalian DNA ligase I through phosphorylation by casein kinase II.. EMBO Journal, EMBO Press, 1992, 11 (8), pp.2925-33. ⟨inserm-00966023⟩



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