Inhibition of DNA binding by the phosphorylation of poly ADP-ribose polymerase protein catalysed by protein kinase C.
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.
Bauer
P I
PI
Department of Biochemistry I, Semmelweis University of Medicine, Budapest, Hungary.
Farkas
G
G
Buday
L
L
Mikala
G
G
Meszaros
G
G
Kun
E
E
Farago
A
A
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D004247:DNA / Q000378:metabolism*; D004789:Enzyme Activation; D007527:Isoenzymes / Q000378:metabolism; D010766:Phosphorylation; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011493:Protein Kinase C / Q000378:metabolism*; D011817:Rabbits
D007527:Isoenzymes; D000255:Adenosine Triphosphate; D004247:DNA; D011065:Poly(ADP-ribose) Polymerases; D011493:Protein Kinase C