ADP-ribosylation of nuclear proteins is increased by phenobarbital. Identification of the ADP-ribosylated histone fractions in rat liver nuclei.
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 Hl and in core histones was evaluated, the specific radioactivities increasing 150, 40 and 8%, respectively. Histones Hl 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.
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Lechner
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D009698:Nucleoproteins / Q000378:metabolism; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D010634:Phenobarbital / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains
D006657:Histones; D009698:Nucleoproteins; D009702:Nucleoside Diphosphate Sugars; D000246:Adenosine Diphosphate Ribose; D010634:Phenobarbital