FEBS Letters | |
A 22 kDa ras‐related G‐protein is the substrate for an ADP‐ribosyltransferase from Clostridium botulinum | |
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
【 预 览 】
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