Modification of proteins by mono(ADP-ribosylation) in vivo

Biochemistry. 1985 Dec 17;24(26):7540-9. doi: 10.1021/bi00347a006.

Abstract

We have pursued the detection of in vivo modified, ADP-ribosylated proteins containing N-glycosylic linkages to arginine. ADP-ribosylated histone, elongation factor 2, and transducin, containing the different known ADP-ribosylated amino acids (arginine, diphthamide, and cysteine, respectively), were employed as model conjugates to establish conditions for the selective detection of adenosine(5')diphosphoribose (ADP-ribose) residues bound to arginine. We report here the detection and quantification of protein-bound ADP-ribose residues in adult rat liver with linkages characteristic of arginine. These mono(ADP-ribose) residues were present in vivo at a level of 31.8 pmol/mg of protein which is 400-fold higher than polymeric ADP-ribose residues. A minor fraction (23%) of the ADP-ribose residues detected were bound via a second, more labile linkage with chemical properties very similar to those described for carboxylate ester linked ADP-ribose.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate Ribose / isolation & purification
  • Adenosine Diphosphate Ribose / metabolism*
  • Animals
  • Arginine / metabolism
  • Hydroxylamine
  • Hydroxylamines / pharmacology
  • Liver / metabolism
  • Nucleoside Diphosphate Sugars / metabolism*
  • Proteins / isolation & purification
  • Proteins / metabolism*
  • Rats

Substances

  • Hydroxylamines
  • Nucleoside Diphosphate Sugars
  • Proteins
  • Adenosine Diphosphate Ribose
  • Hydroxylamine
  • Arginine