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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Bràz J,Lechner MC

doi

10.1016/0014-5793(86)80472-0

subject

Has Abstract

pub_date

1986-04-21 00:00:00

pages

164-8

issue

2

eissn

0014-5793

issn

1873-3468

journal_volume

199

pub_type

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