Presence of poly (ADP‐ribose) polymerase and poly (ADP‐ribose) glycohydrolase in the dinoflagellate Crypthecodinium cohnii

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Abstract
Poly(ADP‐ribose) polymerase and poly(ADP‐ribose) glycohydrolase have been detected in chromatin extracts from the dinoflagellate Crypthecodinium cohnii. Poly(ADP‐ribose) glycohydrolase was detected by the liberation of ADP‐ribose from poly(ADP‐ribose). Poly(ADP‐ribose) polymerase was proved by (a) demonstration of phosphoribosyl‐AMP in the phosphodiesterase digest of the reaction product, (b) demonstratioin of ADP‐ribose oligomers by fractionation of the reaction product on DEAE‐Sephadex. The (ADP‐ribose)‐protein transfer is dependent on DNA; it is inhibited by nicotinamide, thymidine, theophylline and benzamide. The protein‐(ADP‐ribose bond is susceptible to 0.1 M NaOH (70 %) and 0.4 M NH2OH (33 %). Dinoflagellates, nucleated protists, are unique in that their chromatin lacks histones and shows a conformation like bacterial chromatin [Loeblich, A. R., III (1976) J. Protozool. 23, 13–281; poly(ADP‐ribose) polymerase, however, has been found only in eucaryotes. Thus our results suggest that histones were not relevant to the establishment of poly(ADP‐ribose) during evolution.