ADP-ribosylation of nuclear proteins is increased by phenobarbital: Identification of the ADP-ribosylated histone fractions in rat liver nuclei

• Published in: FEBS letters Vol. 199; no. 2; pp. 164 - 168
• Main Authors: Bràz, Judite, Celeste Lechner, Maria
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 21.04.1986; Elsevier
• Subjects: Adenosine Diphosphate Ribose - metabolism; ADP-ribosylation; Animals; Applied sciences; Biological and medical sciences; Electrophoresis, Polyacrylamide Gel; Exact sciences and technology; General and cellular metabolism. Vitamins; Histone; Histones - isolation & purification; Histones - metabolism; Liver - drug effects; Liver - metabolism; Male; Medical sciences; Molecular Weight; Nuclear protein; Nucleoproteins - metabolism; Nucleoside Diphosphate Sugars - metabolism; Other techniques and industries; Pharmacology. Drug treatments; Phenobarbital - pharmacology; Phenobarbital stimulation; Rats; Rats, Inbred Strains; Histone; Phenobarbital stimulation; Nuclear protein; ADP-ribosylation; Ribosylation; ADP; Barbituric
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(86)80472-0

Changes in the ADP-ribosylation of total proteins and purified histones of rat liver nuclei after phenobarbital treatment (80 mg kg , 24 h) have been studied. The [ 32P]NAD incorporation into total trichloroacetic acid precipitated proteins, in histone H1 and in core histones was evaluated, the specific radioactivities increasing 150, 40 and 8%, respectively. Histones H1 and H2B were the best ADP-ribose acceptors. Histone H4 did not show any 32P incorporation, as revealed by autoradiography after SDS-PAGE of the purified histones, in either the control or phenobarbital treated rats. Possible involvement of ADP-ribosylation of nuclear proteins in the adaptative response of liver to phenobarbital is discussed.