Increased thermal stability of solubilized chromatin after poly(ADP-ribose) synthesis.
A hyperthermic shift in the hyperchromicity curve of thermally denatured swine aortic-smooth-muscle-cell chromatin solubilized by digestion of nuclei with micrococcal nuclease was observed after the chromatin was incubated under conditions to allow poly-(ADP-ribose) synthesis by the endogenous poly(ADP-ribose) polymerase. When the order of solubilization and poly(ADP-ribosyl)ation was reversed, a smaller proportion of the solubilized chromatin exhibited greater thermal stability. Nuclease digestion of nuclei preincubated for poly(ADP-ribose) synthesis revealed no difference in kinetics of digestion or fragment size distribution compared to that of control nuclei. Poly(ADP-ribose) synthesis in these nuclei was proportionately greater in the chromatin fraction most resistant to solubilization by micrococcal nuclease treatment.
D000818:Animals; D001011:Aorta; D002843:Chromatin / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D004355:Drug Stability; D006358:Hot Temperature; D008836:Micrococcal Nuclease; D009131:Muscle, Smooth, Vascular / Q000648:ultrastructure*; D009691:Nucleic Acid Denaturation; D009702:Nucleoside Diphosphate Sugars / Q000096:biosynthesis*; D011064:Poly Adenosine Diphosphate Ribose / Q000096:biosynthesis*; D012995:Solubility; D013552:Swine
D002843:Chromatin; D009702:Nucleoside Diphosphate Sugars; D011064:Poly Adenosine Diphosphate Ribose; D004247:DNA; D008836:Micrococcal Nuclease