Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin.
The culture medium of certain strains of Clostridium botulinum type C contains two separable ADP-ribosyltransferases. Besides the ADP-ribosylation of actin due to botulinum C2 I toxin, a second microbial enzyme causes the mono-ADP-ribosylation of a eukaryotic protein with a molecular mass of about 20 kDa found in platelets, neuroblastoma X glioma hybrid cells, S49 lymphoma cells, chick embryo fibroblasts and sperm. The eukaryotic substrate is inactivated by heating and trypsin treatment. In contrast, the novel ADP-ribosyltransferase, which can be separated by DEAE-Sephadex chromatography, is largely resistant in the short term to trypsin digestion.
D036002:ADP Ribose Transferases; D000199:Actins / Q000378:metabolism; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000818:Animals; D001905:Botulinum Toxins / Q000096:biosynthesis* / Q000302:isolation & purification; D003014:Clostridium botulinum / Q000201:enzymology* / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D010430:Pentosyltransferases / Q000096:biosynthesis*; D011506:Proteins / Q000378:metabolism; D014357:Trypsin
D000199:Actins; D011506:Proteins; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; D010430:Pentosyltransferases; D014357:Trypsin; D001905:Botulinum Toxins