Bortell, RitaRigby, Mark R.Stevens, Linda A.Moss, JoelKanaitsuka, ToshihiroMordes, John P.Greiner, Dale L.Rossini, Aldo A.2022-08-232022-08-231997-01-012008-08-05Adv Exp Med Biol. 1997;419:169-73.0065-2598 (Print)9193650https://hdl.handle.net/20.500.14038/32566We report that rat RT6.2 and recombinant mouse Rt6 locus 1 proteins possess auto-ADP-ribosyltransferase activity and that Rt6, but not RT6, catalyzes the ADP-ribosylation of exogenous histones. Based on NH2OH sensitivity, it appeared that the ADP-ribose was attached to arginine residues on proteins. We also observed that the NAD+ concentration in culture medium correlates inversely with the proliferation of rat RT6+ T cells. The data suggest that lymphocyte surface ADP-ribosyltransferases could be involved in signaling and immunoregulatory processes.en-USMouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activityJournal Articlehttps://escholarship.umassmed.edu/gsbs_sp/113566367gsbs_sp/113