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ADP-ribosylation of small GTP-binding proteins by Bacillus cereus
I Just1, G Schallehn, K Aktories
1Institut für Pharmakologie und Toxikologie, Universität des Saarlandes, Homburg-Saar, FRG.
Biochemical and Biophysical Research Communications
|March 31, 1992
Abstract:
A human pathogenic strain of Bacillus cereus produces an exoenzyme which selectively ADP-ribosylates 20-25 kDa GTP-binding proteins in platelet membranes. Pre-ADP-ribosylation of rho proteins of human platelet membranes with Clostridium botulinum exoenzyme C3 or Clostridium limosum exoenzyme inhibits subsequent ADP-ribosylation by the exoenzyme from B. cereus indicating similar substrate specificity of the transferases. The ADP-ribosyltransferase from B. cereus reveals no immunological cross-reactivity with C. botulinum C3 and C. limosum exoenzyme.