Modification of proteins by mono(ADP-ribosylation) in vivo.
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.
D000246:Adenosine Diphosphate Ribose / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D001120:Arginine / Q000378:metabolism; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D008099:Liver / Q000378:metabolism; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism*; D011506:Proteins / Q000302:isolation & purification / Q000378:metabolism*; D051381:Rats
D006898:Hydroxylamines; D009702:Nucleoside Diphosphate Sugars; D011506:Proteins; D000246:Adenosine Diphosphate Ribose; D019811:Hydroxylamine; D001120:Arginine