Molecular Characterization of Rat T Lymphocyte Alloantigen RT6.1 as an ADP-Ribosyltransferase

  • Tomohiko Maehama
  • Toshiaki Katada
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 419)


A family of glycosylphosphatidylinositol-linked ADP-ribosyltransferases, of which cDNAs were cloned from various mammalian cells, possess a common Glu-rich motif (EEEVLIP) near their carboxyl termini. Although the first Glu in the common motif is replaced by Gln (Q207EEVLIP) in rat T lymphocyte alloantigens RT6.1 and RT6.2, the two RT6s appear to have ADP-ribosyltransferase activity. To investigate the significance of the Glu-rich motif in the enzyme activity, we produced a mutant RT6.1, in which Gln207 was replaced by Glu (Q207E), together with wild-type RT6s, in Escherichia coli. The recombinant RT6.1 and RT6.2 displayed extremely low auto-ADP-ribosylation, though the latter modification was somewhat higher than the former one. In contrast, much higher the auto-modification was observed for Q207E mutant. Moreover, the mutant could effectively ADP-ribosylate agmatine as a substrate. Thus, the single amino acid mutation of RT6.1 caused remarkable increase in its ADP-ribosyltransferase activity, indicating that the Glu-rich motif near the carboxy terminus plays an important role in the enzyme activity.


Nicotinamide Adenine Dinucleotide Carboxyl Terminus Nicotinamide Adenine Dinucleotide Carboxy Terminus Common Motif 
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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Tomohiko Maehama
    • 1
  • Toshiaki Katada
    • 1
  1. 1.Department of Physiological Chemistry Faculty of Pharmaceutical SciencesUniversity of TokyoHongo, Tokyo 113Japan

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