Alkylation-induced mono(ADP-ribosyl)-histones H1 and H2B. Hydroxylamine-resistant linkage in hepatoma cells.
Treatment of hepatoma AH 7974 cells with dimethyl sulfate led to a marked accumulation in vivo of mono)ADP-ribosyl)-histone H1A, H1B, H1 and H2B, respectively. In these conjugates, most of the modifying groups were linked to the acceptor proteins by an 'unusual' bond not described so far for ADP-ribosyl histone conjugates. It resisted treatment with 3M hydroxylamine, 0.1M picrylsulfonate and mild alkali, which excluded a linkage through carboxyl or guanidino residues. The stability of these conjugates formed endogenously differed also from 'non-enzymic' histone H1 conjugates formed by incubation of free ADP-ribose with the histone. Histone-linked mono(ADP-ribosyl) residues synthesized in hepatoma cells in response to alkylation were located exclusively in the domains that interact with DNA, i.e. in the non-globular C-terminal tail of histone H1 and in the N-terminus of histone H2B. Besides poly(ADP-ribosyl)ation, the modification of histones by single ADP-ribose groups may represent an independent process to modulate DNA/histone interaction.
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000478:Alkylation; D000818:Animals; D002460:Cell Line; D055598:Chemical Phenomena; D002621:Chemistry; D004247:DNA / Q000378:metabolism; D005260:Female; D006657:Histones / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013463:Sulfuric Acid Esters / Q000494:pharmacology
D006657:Histones; D006898:Hydroxylamines; D009702:Nucleoside Diphosphate Sugars; D010446:Peptide Fragments; D013463:Sulfuric Acid Esters; D000246:Adenosine Diphosphate Ribose; D019811:Hydroxylamine; D004247:DNA; C007482:dimethyl sulfate