ADP-ribosylation of core histones and their acetylated subspecies.
ADP-ribosylation of core histones was investigated in isolated nuclei of Physarum polycephalum. Core histone species differed in the mode of modification. Whereas ADP-ribosylation of H2A and H2B is sensitive to inhibition by 3-methoxybenzamide, as with most other nuclear acceptor proteins, the modification of H3 and H4 is not inhibited. Cleavage experiments with hydroxylamine indicate a carboxylate ester type ADP-ribose-protein bond for H2A and H2B and arginine-linked ADP-ribose residues for H3 and H4. ADP-ribosylation preferentially occurs on acetylated histone subspecies, as shown for H4. These data are substantiated by the use of n-butyrate, which induces hyperacetylation of core histones; the butyrate-induced shift towards more acetylated H4 subspecies is accompanied by an increase of ADP-ribose incorporation into highly acetylated H4 subspecies.
Golderer
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G
Institut für Medizinische Chemie und Biochemie der Universität, Innsbruck, Austria.
Gröbner
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P
D000107:Acetylation; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D001549:Benzamides / Q000494:pharmacology; D005656:Fungal Proteins / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006358:Hot Temperature; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000737:chemistry; D010804:Physarum
D001549:Benzamides; D005656:Fungal Proteins; D006657:Histones; D006898:Hydroxylamines; D000246:Adenosine Diphosphate Ribose; D019811:Hydroxylamine; C037689:benzamide; C025160:3-aminobenzamide; C025159:3-methoxybenzamide