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Poly (ADP-ribose) synthetase is phosphorylated by protein kinase C in vitro
Y Tanaka1, S S Koide, K Yoshihara
1Department of Biochemistry, Nara Medical University, Japan.
Biochemical and Biophysical Research Communications
|October 29, 1987
Abstract:
Poly (ADP-ribose) synthetase from bovine thymus was phosphorylated effectively by protein kinase C in vitro. The phosphorylation was dependent on the activators of this kinase, Ca2+ and phospholipid. The apparent Km for the synthetase was about 8 microM, which was lower than that for histone H1. Though the synthetase was a weak substrate for Ca2+/calmodulin-dependent protein kinase II, other protein kinases, cyclic AMP-dependent and cofactor-independent protein kinases did not phosphorylate the synthetase. Phosphorylation of the synthetase by protein kinase C resulted in appreciable inhibition of the synthetase activity.