ADP-ribosylation of small GTP-binding proteins by Bacillus cereus.
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.
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Institut für Pharmakologie und Toxikologie, Universität des Saarlandes, Homburg-Saar, FRG.
Schallehn
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Aktories
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D036002:ADP Ribose Transferases / Q000276:immunology / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000378:metabolism; D001409:Bacillus cereus / Q000201:enzymology*; D001792:Blood Platelets / Q000378:metabolism; D001905:Botulinum Toxins; D003013:Clostridium / Q000201:enzymology; D003429:Cross Reactions; D019204:GTP-Binding Proteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000276:immunology / Q000378:metabolism*; D013379:Substrate Specificity
D008565:Membrane Proteins; D000244:Adenosine Diphosphate; D036002:ADP Ribose Transferases; C063007:exoenzyme C3, Clostridium botulinum; D011065:Poly(ADP-ribose) Polymerases; D001905:Botulinum Toxins; D019204:GTP-Binding Proteins