Normal and crown gall tumor tissue cultures of tobacco had poly(ADP-ribose) polymerase associated with the chromatin and two poly(A) polymerases (separable by DEAE-Sephadex A-25 chromatography) with the soluble fraction. The two poly(A) polymerases resembled mammalian enzymes in molecular mass (65-70 kDa), K,,,*rP (0.1-0.2 mM), primer and substrate preference (poly(A) and ATP, respectively), pH optimum (8-8.5) cation requirement (0.25 mM Mr?+/l mM Mg2+ = 5-15) inhibition by 3'-dATP and sperrnine and lack of inhibition by cc-amanatin. Likewise the tobacco tumor tissue contained 4-times higher activities of both poly(A) polymerases and 6-times higher activity of poly(ADP-ribose) polymerase as compared to the normal tissue indicating their enhanced function in transformed cells.