IDENTIFICATION IN HUMAN ERYTHROCYTES OF MONO(ADP-RIBOSYL) PROTEIN HYDROLASE THAT CLEAVES A MONO(ADP-RIBOSYL) G1 LINKAGE

被引：30

作者：

TANUMA, S

ENDO, H

机构：

[1] Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa

来源：

FEBS LETTERS | 1990年 / 261卷 / 02期

关键词：

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

D O I：

10.1016/0014-5793(90)80597-C

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A novel enzymatic activity, the hydrolysis of linkages between mono(ADP-ribose) and cysteine residues in Gi 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) Gi 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) 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. © 1990.

引用

页码：381 / 384

页数：4

共 14 条

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