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

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Abstract
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.

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