[ADP-ribosylation of histones of the chicken liver nucleus at different rates of glycohydrolase hydrolysis of NAD].
The rate of incorporation of nicotinamide-[adenosine-U-14C]adenine dinucleotide [( Ado-U-14C]NAD) into histones and the poly(ADPR) polymerase activity of chromatin suggest that the NAD-dependent ADP-ribosylation of histones depends on the rate of NAD hydrolysis by glycohydrolase in chicken liver nuclei. With a rise in the NAD-glycohydrolase activity after treatment of nuclei with Triton X-100 the synthesis of poly(ADP-ribose) via the poly(ADPR)polymerase reaction is augmented, as a result of which the rate of [Ado-U-14C]NAD incorporation into total histones is increased. On the contrary, the decrease of NAD-glycohydrolase hydrolysis after treatment of nuclei with SDS lowers the poly(ADPR)polymerase activity and [Ado-U-14C]NAD incorporation into histones. Under these conditions, i. e. different rates of glycohydrolase hydrolysis of NAD in the nuclei, some redistribution of [Ado U-14C]NAD incorporation into individual histones occurs.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D002645:Chickens; D006657:Histones / Q000378:metabolism*; D006868:Hydrolysis; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D009243:NAD / Q000378:metabolism*; D009244:NAD+ Nucleosidase / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*
D006657:Histones; D009243:NAD; D011065:Poly(ADP-ribose) Polymerases; D009699:N-Glycosyl Hydrolases; D009244:NAD+ Nucleosidase
ADP-ribozilirovanie gistonov iader pecheni tsypliat pri razlichnoĭ intensivnosti glikogidrolaznogo raspada NAD.