Mouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activity

Adv Exp Med Biol. 1997;419:169-73.

Abstract

We 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.

MeSH terms

  • ADP Ribose Transferases / genetics
  • ADP Ribose Transferases / metabolism*
  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Antigens, Differentiation, T-Lymphocyte
  • Catalysis
  • Cell Division
  • Cell Line
  • Genetic Linkage
  • Histocompatibility Antigens / genetics
  • Histocompatibility Antigens / metabolism*
  • Membrane Glycoproteins*
  • Mice
  • NAD / metabolism*
  • NAD / pharmacology
  • Precipitin Tests
  • Rats
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Spodoptera / cytology
  • T-Lymphocytes / cytology

Substances

  • Antigens, Differentiation, T-Lymphocyte
  • Histocompatibility Antigens
  • Membrane Glycoproteins
  • Recombinant Fusion Proteins
  • NAD
  • Adenosine Diphosphate Ribose
  • ADP Ribose Transferases
  • Art2b protein, mouse
  • Art2b protein, rat