ADP-ribosylation regulates the phosphorylation of histones by the catalytic subunit of cyclic AMP-dependent protein kinase.
Phosphorylation of whole histones from calf thymus by the catalytic subunit of cyclic AMP-dependent protein kinase was markedly reduced when the histones were ADP-ribosylated. NAD, nicotinamide or free ADP-ribose molecule did not suppress the phosphorylation. Urea gel electrophoretic analyses of the phosphorylated histones which had already been ADP-ribosylated revealed that the suppression of phosphorylation occurred in both H1 and core histones. Therefore, the possibility that ADP-ribosylation may regulate the phosphorylation of histones phosphorylation in nuclei warrants further investigation.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002467:Cell Nucleus / Q000201:enzymology; D002645:Chickens; D005260:Female; D006657:Histones / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins; D008099:Liver / Q000201:enzymology; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D009713:Nucleotidyltransferases / Q000378:metabolism*; D010766:Phosphorylation; D011065:Poly(ADP-ribose) Polymerases; D011494:Protein Kinases / Q000378:metabolism*; D013950:Thymus Gland / Q000201:enzymology
D002352:Carrier Proteins; D006657:Histones; D047908:Intracellular Signaling Peptides and Proteins; D009702:Nucleoside Diphosphate Sugars; C015482:protein kinase modulator; D000246:Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases; D011494:Protein Kinases; D009713:Nucleotidyltransferases