Stimulatory effect of histones on phosphorylation of nuclear phosphoproteins.
Effect of histones on phosphorylation of nuclear phosphoproteins was studied using two species of phosphoprotein kinases with different kinetic and catalytic properties; namely, protein kinases A1 and A2 (Takeda, M., Matsumura, S., & Nakaya, Y. (1974) J. Biochem. 75, 743-751). The reaction rate for protein kinase A1 was markedly enhanced when histone or polylysine was added to the reaction mixture. Analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the basic protein served as a stimulator rather than acted as a substrate in this reaction. In contrast, when protein kinase A2 was employed, the stimulatory action of these basic proteins was less marked than for protein kinase A1. It seems likely that the phosphorylation of nuclear phosphoproteins, particularly the reaction catalyzed by protein kinase A1, may be strongly influenced by histones which are integrated in the chromatin structure.
D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D006657:Histones / Q000494:pharmacology*; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D008970:Molecular Weight; D011107:Polylysine / Q000494:pharmacology; D006656:Protamine Kinase / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats
D002868:Chromosomal Proteins, Non-Histone; D006657:Histones; D011107:Polylysine; D011494:Protein Kinases; D006656:Protamine Kinase