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Journal Articles EMBO Journal Year : 1992

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

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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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inserm-00966023 , version 1 (26-03-2014)

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

Cite

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, 1992, 11 (8), pp.2925-33. ⟨inserm-00966023⟩

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