Identification in human erythrocytes of mono(ADP-ribosyl) protein hydrolase that cleaves a mono(ADP-ribosyl) Gi linkage.
A novel enzymatic activity, the hydrolysis of linkages between mono(ADP-ribose) and cysteine residues in Gi prepared by eukaryotic ADP-ribosyltransferase C [(1988) J. Biol. Chem. 263, 5485-5489] was found in the cytosol of human erythrocytes. The mono(ADP-ribosyl) Gi hydrolase, tentatively named ADP-ribosyl protein hydrolase C was partially purified by sequential chromatographies on DEAE-cellulose and Blue Sepharose. This enzyme catalyzes the release of ADP-ribose from mono(ADP-ribosyl) Gi. Its activity was enhanced by Ca2+ and inhibited by ADP-ribose. The presence of this enzyme in eukaryotic cells suggests that endogenous mono(ADP-ribosyl)ation of Gi is a reversible post-translational modification.
Tanuma
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Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Kanagawa, Japan.
Endo
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D000246:Adenosine Diphosphate Ribose / Q000097:blood* / Q000494:pharmacology; D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D004912:Erythrocytes / Q000201:enzymology*; D019204:GTP-Binding Proteins / Q000097:blood*; D006801:Humans; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000097:blood*; D006868:Hydrolysis; D007700:Kinetics
D000246:Adenosine Diphosphate Ribose; D006867:Hydrolases; C063440:ADP-ribosyl protein hydrolase C; D019204:GTP-Binding Proteins