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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Article dans une revue
EMBO J, 1992, 11 (8), pp.2925-33
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Contributeur : Claude Prigent <>
Soumis le : mercredi 26 mars 2014 - 08:23:22
Dernière modification le : mercredi 26 mars 2014 - 10:28:31

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

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

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