A 22 kDa ras‐related G‐protein is the substrate for an ADP‐ribosyltransferase from Clostridium botulinum

FEBS Letters

Brown, Joan Heller²  Quilliam, Lawrence A.²  Buss, Janice E.¹ 

[1] La Jolla Cancer Research Foundation, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA;Department of Pharmacology M-036, University of California San Diego, La Jolia, CA 92093, USA

关键词: ADP-ribosylation;    Botulinum toxin;    GTP-binding protein;    ras gene;    BTx;    botulinum toxin type D preparation;    G-protein;    GTP-binding protein;    Gs;    Gi;    stimulatory and inhibitory G-proteins of adenylate cyclase;    GTPγS;    guanosine 5′-O-(3-thiotriphosphate);    GDPβS;    guanosine 5′-O-(2-thiodiphosphate);    p22;    22 kDa BTx substrate;   

DOI  :  10.1016/0014-5793(88)80217-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A ribosyltransferase from C. botulinum type D ADP-ribosylated a protein of 22 kDa (p22) in human astrocytoma (1321N1) cells. ADP-ribosylation of membrane-bound p22 was potentiated by 2 mM MgCl² or guanine nucleotides but was much reduced in the presence of 10 mM Mg²⁺ plus GTPγS. p22 was immunoprecipitated by a monoclonal antibody 142-24E05 raised against a peptide sequence common to the ras gene family but not by other ras or G-protein antibodies. p22 was also ADP-ribosylated in Drosophila but was not detected in Diclyostelium. These data suggest that the 22 kDa botulinum toxin substrate is a GTP-binding protein and a member of the ras protein family.

【 授权许可】

Unknown