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

Lawrence A. Quilliam, Joan Heller Brown, Janice E. Buss

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)22-26
Number of pages5
JournalFEBS Letters
Volume238
Issue number1
DOIs
StatePublished - Sep 26 1988

Keywords

  • ADP-ribosylation
  • Botulinum toxin
  • GTP-binding protein
  • ras gene

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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