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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)

Abstract

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.

Keywords

Nicotinamide Adenine Dinucleotide Carboxyl Terminus Nicotinamide Adenine Dinucleotide Carboxy Terminus Common Motif 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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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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