The Bond

  • Felix R. Althaus
  • Christoph Richter
Part of the Molecular Biology Biochemistry and Biophysics book series (MOLECULAR, volume 37)


Enzymes of bacterial viruses, and prokaryotic and eukaryotic cells catalyze the transfer of ADP-ribose form NAD+ to specific acceptor proteins. In addition to these true ADP-ribosyltransferase reactions, ADP-ribose-acceptor adducts can result from a nonenzymatic reaction between free ADP-ribose and certain acceptor sites, e.g. by Schiff base formation at lysine, arginine, or histidine residues. For an understanding of the roles of enzymatic or nonenzymatic ADP-ribosyltransferase reactions a knowledge of the chemical nature of the ADP-ribose-protein linkage present in vivo, the way in which it is formed and broken, as well as the identity of the acceptor sites is required. In the case of most viral and bacterial ADP-ribosyltransferases the acceptor proteins for ADP-ribose have been clearly identified, often including the amino acid residue (glutamic acid, diphthamide, arginine, cysteine) serving as the site of modification. The exact chemical nature of the bond between the amino acid residue and ADP-ribose has been elucidated in two cases. First, when nuclei are incubated in vitro with NAD+ , histones are mono-ADP-ribosylated, presumably by poly-ADP-ribose polymerase, via ester linkages to the gamma-carboxyl group of glutamic acid residues and to the alpha-carboxyl group of terminal lysine residues (Riquelme et al. 1979; Burzio et al. 1979; Ogata et al. 1980 a, b). Second, the bond formed by diphtheria toxin between diphthamide and ADP-ribose has been clearly identified (van Ness et al. 1980 a, b).


Pertussis Toxin Diphtheria Toxin Rhodospirillum Rubrum Acceptor Protein Guanidino Group 
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Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • Felix R. Althaus
    • 1
  • Christoph Richter
    • 2
  1. 1.Institut für Pharmakologie und BiochemieUniversität ZürichZürichGermany
  2. 2.Laboratorium für BiochemieETH-ZentrumZürichGermany

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