Expression and Comparative Analysis of Recombinant Rat and Mouse RT6 T Cell Mono(ADP-Ribosyl)Transferases In E. Coli

  • Stefan Karsten
  • Jens Schröder
  • Cristina Da Silva
  • Dominik Kahlke
  • Heinz-Günter Thiele
  • Friedrich Koch-Nolte
  • Friedrich Haag
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 419)


Recombinant RT6 proteins of rat and mouse were analyzed for NAD-metabolizing, i.e. mono(ADP-ribosyl)transferase, NAD-glycohydrolase (NADase) and ADP-ribosyl cyclase activities. The results reveal surprising intra- as well as inter-species differences in enzyme activities. While mouse Rt6 proteins were found to be strong arginine-specific transferases, but comparatively weak NADases, the opposite held true for rat RT6, for which transferase activity could only be detected in the form of arginine-specific autoADP-ribosylation, displayed by RT6.2 but not by RT6.1. NADase activity of rat RT6 was not accompanied by production of cyclic ADPR (cADPR). Rat RT6 gained potent arginine-specific transferase activity by exchange of a single amino acid for the corresponding residue of the mouse proteins.


Nicotinamide Adenine Dinucleotide Transferase Activity Nicotinamide Adenine Dinucleotide Single Amino Acid Residue Determine Enzyme Activity 
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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Stefan Karsten
    • 2
  • Jens Schröder
    • 2
  • Cristina Da Silva
    • 1
  • Dominik Kahlke
    • 2
  • Heinz-Günter Thiele
    • 2
  • Friedrich Koch-Nolte
    • 2
  • Friedrich Haag
    • 2
  1. 1.Department of Physiological ChemistryHamburg UniversityHamburgGermany
  2. 2.Department of ImmunologyUniversity Hospital Hamburg-EppendorfHamburgGermany

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