Identification in human erythrocytes of mono(ADP‐ribosyl) protein hydrolase that cleaves a mono(ADP‐ribosyl) Gi linkage

FEBS Letters

Endo, Hiroyoshi¹  Tanuma, Sei-ichi¹ 

[1] Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa 199-01, Japan

关键词: Endogenous mono(ADP-ribosyl)ation;    Mono(ADP-ribosyl) protein hydrolase;    Mono(ADP-ribosyl)transferase;    GTP-binding protein;    Signal transduction;   

DOI  :  10.1016/0014-5793(90)80597-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel enzymatic activity, the hydrolysis of linkages between mono(ADP-ribose) and cysteine residues in G_i prepared by eukaryotic ADP-ribosyl-transferase C [(1988) J. Biol. Chem. 263, 5485-5489] was found in the cytosol of human erythrocytes. The mono(ADP-ribosyl) G_i hydrolase, tentatively named ADP-ribosyI 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) G_i 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 G_i is a reversible post-translational modification.

【 授权许可】

Unknown