Mono (ADP-ribosyl)ation of hen liver nuclear proteins suppresses phosphorylation.
The phosphorylation of nuclear proteins from hen liver nuclei was suppressed under conditions of incubation with NAD. The reconstituted protein kinase assay system containing heat-treated and subsequently ADP-ribosylated nuclei and NI type protein kinase revealed that the ADP-ribosylated nuclear proteins are poor acceptors for the phosphorylation reaction. Therefore, mono(ADP-ribosyl)ation may contribute to the regulation of phosphorylation reaction in nuclei.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D005260:Female; D006358:Hot Temperature; D008099:Liver / Q000378:metabolism*; D009698:Nucleoproteins / Q000378:metabolism*; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D010766:Phosphorylation
D009698:Nucleoproteins; D009702:Nucleoside Diphosphate Sugars; D000246:Adenosine Diphosphate Ribose