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ADP‐ribosylation regulates the phosphorylation of histones by the catalytic subunit of cyclic AMP‐dependent protein kinase
Author(s) -
Tanigawa Yoshinori,
Mikako Tsuchiya,
Yasuki Imai,
Makoto Shimoyama
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80970-3
Subject(s) - phosphorylation , histone , adp ribosylation , protein kinase a , nad+ kinase , biochemistry , nicotinamide , protein subunit , chemistry , protein phosphorylation , kinase , microbiology and biotechnology , biology , enzyme , dna , gene
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.