title: Mono(ADP-ribosylation) in rat liver mitochondria.
abstract: This paper investigates protein mono(ADP-ribosylation) in rat liver mitochondria. In isolated inner mitochondrial membranes, in the presence of both ADP-ribose and NAD+, a protein is mono-(ADP-ribosylated) with high specificity. The reaction apparently consists of enzymatic NAD+ glycohydrolysis and subsequent binding of free ADP-ribose to the acceptor protein. In terms of chemical stability, the resulting bond is unique among the ADP-ribose linkages thus far characterized. Formation of a Schiff base adduct between free ADP-ribose and the acceptor protein is excluded. In intact mitochondria at least three classes of proteins are ADP-ribosylated in vivo. One ADP-ribose-protein linkage is of the carboxylate ester type as indicated by its lability in neutral buffer. Another class of ADP-ribosylated proteins requires hydroxylamine for release of ADP-ribose. The third class is stable in hydroxylamine but labile to alkali, similar to the ADP-ribose-cysteine linkage in transducin formed by pertussis toxin.
authors.affiliation: Laboratorium für Biochemie, Eidgenössische Technische Hochschule, Zürich, Switzerland.
authors.forename: B
authors.initials: B
authors.lastname: Frei
authors.forename: C
authors.initials: C
authors.lastname: Richter
mesh_terms: D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D007425:Intracellular Membranes / Q000378:metabolism; D007700:Kinetics; D008930:Mitochondria, Liver / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D009244:NAD+ Nucleosidase / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D051381:Rats; D013367:Submitochondrial Particles / Q000378:metabolism*
chemical_list: D006898:Hydroxylamines; D011506:Proteins; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D019811:Hydroxylamine; D009244:NAD+ Nucleosidase