Modulation of chromatin superstructure induced by poly(ADP-ribose) synthesis and degradation.
It has been demonstrated recently by Poirier et al. (Poirier, G. G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C., and Mandel, P. (1982) Proc. Natl. Acad. Sci. U.S.A. 79, 3423-3427) that poly(ADP-ribosyl)ation of pancreatic nucleosomes causes relaxation of the chromatin superstructure through H1 modification. The in vitro effect of poly(ADP-ribose) synthesis and degradation on calf thymus chromatin was investigated by the time course incorporation of ADP-ribose, electron microscopy, analytical ultracentrifugation, and autoradiography of the protein acceptors. Purified calf thymus poly(ADP-ribose) polymerase and partially purified bull testis poly(ADP-ribose) glycohydrolase were used. Degradation of ADP-ribose units on hyper(ADP-ribosyl)ated H1 by poly(ADP-ribose) glycohydrolase restores the native condensed chromatin superstructure. This reversible conformational change induced by poly(ADP-ribosyl)ation on nucleosomal arrangement could be one of the mechanisms by which the accessibility of DNA polymerases and/or excision-repair enzymes is favored, the native structure being fully restorable.
D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism / Q000648:ultrastructure*; D007700:Kinetics; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D009707:Nucleosomes / Q000378:metabolism; D011064:Poly Adenosine Diphosphate Ribose / Q000096:biosynthesis / Q000378:metabolism*; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D013950:Thymus Gland / Q000378:metabolism
D002843:Chromatin; D009702:Nucleoside Diphosphate Sugars; D009707:Nucleosomes; D011064:Poly Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases