Poly(ADP-ribose) effectively competes with DNA for histone H4 binding.
The effect of poly(ADP-ribose) on DNA-histone H4 interaction was studied using a nitrocellulose filter binding assay. Poly-(ADP-ribose) was found to form poly(ADP-ribose)-histone H4 complexes at physiological salt concentrations. The homopolymer effectively competed with DNA for histone H4 binding. Poly(ADP-ribose) was also capable of displacing DNA from preformed DNA-histone H4 complexes. Our hypothesis is that poly(ADP-ribose), locally and transiently formed at the site of DNA damage, causes dissociation of DNA from the nucleosome particle or nucleosome unfolding.
D000818:Animals; D001667:Binding, Competitive; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000032:analysis; D008957:Models, Genetic; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D011064:Poly Adenosine Diphosphate Ribose / Q000378:metabolism*; D051381:Rats
D006657:Histones; D009702:Nucleoside Diphosphate Sugars; D011064:Poly Adenosine Diphosphate Ribose; D004247:DNA