ADP‐ribosylation regulates the phosphorylation of histones by the catalytic subunit of cyclic AMP‐dependent protein kinase
- 22 August 1983
- journal article
- Published by Wiley in FEBS Letters
- Vol. 160 (1-2) , 217-220
- https://doi.org/10.1016/0014-5793(83)80970-3
Abstract
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.Keywords
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