Enhanced template activity in chromatin from adrenal medulla after phosphorylation of chromosomal proteins.
Translocation of protein kinase to the nucleus had been implicated earlier in the transsynaptic control of gene expression mediated by cholinergic nerves in adrenal medulla. Phosphorylation of chromosomal proteins by adenosine 3',5'-monophosphate-dependent protein kinase and adenosine 3',5'-monophosphate enhances the template activity of chromatin from adrenal medulla. When homologous RNA polymerase II is used the relative activation is greater than that obtained with Escherichia coli RNA polymerase. The substrate for such phosphorylation does not seem to be RNA polymerase II. Phosphorylation of specific acidic protein probably mediates this enhancement of template activity.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000313:Adrenal Medulla / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002474:Cell-Free System; D002843:Chromatin / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D003852:Deoxyribonucleoproteins / Q000378:metabolism*; D009698:Nucleoproteins / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D012333:RNA, Messenger / Q000096:biosynthesis*; D013698:Templates, Genetic
D002843:Chromatin; D003852:Deoxyribonucleoproteins; D009698:Nucleoproteins; D010710:Phosphates; D012333:RNA, Messenger; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D011494:Protein Kinases; D012321:DNA-Directed RNA Polymerases