Stimulation by polydeoxyribonucleotide of histone phosphorylation by guanosine 3':5'-monophosphate-dependent protein kinase.

Abstract The phosphorylation of histone by cyclic GMP-dependent protein kinase (protein kinase G) was markedly enhanced by polydeoxyribonucleotide with the chain length of several nucleotides up to highly polymerized DNA. Such enhancement was observed for the phosphorylation of H2A, H2B, H3 and H4 histone fractions. The reaction with H1 histone was always inhibited. On the other hand, polydeoxyribonucleotide was inhibitory for the reactions of cyclic AMP-dependent protein kinase (protein kinase A) irrespective of histone fractions employed. The result raises a possibility that the histones associated with nucleosome structure may serve as preferable substrates for protein kinase G rather than for protein kinase A.