Inhibition of DNA binding by the phosphorylation of poly ADP-ribose polymerase protein catalysed by protein kinase C

Biochem Biophys Res Commun. 1992 Sep 16;187(2):730-6. doi: 10.1016/0006-291x(92)91256-p.


Purified type II (beta) and type III (alpha) protein kinase C phosphorylates highly purified polyADP-ribose polymerase in vitro whereby 2 mols of phosphate are transferred from ATP to serine and threonine residues present in the 36 and 56 kDa polypeptide domains of the polymerase protein. Calf thymus DNA was a non-competitive inhibitor of the protein kinase C catalyzed phosphorylation of polyADP-ribose polymerase. Coincidental with the phosphorylation of the protein the polymerase activity and DNA binding capacity of polyADP-ribose polymerase were inhibited. These in vitro findings may have possible cell biological significance in cellular signal transduction.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Cattle
  • DNA / metabolism*
  • Enzyme Activation
  • Isoenzymes / metabolism
  • Phosphorylation
  • Poly(ADP-ribose) Polymerases / metabolism*
  • Protein Kinase C / metabolism*
  • Rabbits


  • Isoenzymes
  • Adenosine Triphosphate
  • DNA
  • Poly(ADP-ribose) Polymerases
  • Protein Kinase C