Dephosphorylation of phosphorylase kinase by a histone H1-stimulated phosphoprotein phosphatase.
A histone H1-stimulated protein phosphatase isolated from rabbit skeletal muscle dephosphorylated [32P]phosphorylase kinase. The rate of dephosphorylation was markedly increased by 5-50 micrograms histone H1/ml. Only the alpha and alpha' subunits were dephosphorylated in the absence or presence of histone H1. This is consistent with previous results suggesting that the H1-stimulated phosphatase is a type-2 protein phosphatase. The present studies suggest that the histone H1-stimulation is the result of a direct interaction of the histone with the phosphatase.
D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D006657:Histones / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010764:Phosphorylase Kinase / Q000378:metabolism*; D011817:Rabbits; D013379:Substrate Specificity
D006657:Histones; D010764:Phosphorylase Kinase; D010749:Phosphoprotein Phosphatases