Bacterial ADP-ribosylating toxins: molecular structures and signal transducing functions.
Mono-ADP-ribosylation is a posttranslational modification of proteins employed by a variety of bacterial ADP-ribosylating toxins to modify the metabolism of target cells. The ADP-ribosyltransferases of bacterial toxins, in general, use NAD as a substrate for covalent modification by ADP-ribose to certain GTP-binding proteins (G proteins) as signal transducers resulting in altered enzymatic activity of the membrane enzymes as effectors. Such a mechanism has the potential of being of importance in the physiological regulation of cellular metabolism, particularly if the process is reversible. These ADP-ribosylating toxins are characterized in Table 1.
Kato
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Department of Oral Bacteriology, School of Dentistry, Showa University, Tokyo.
D036002:ADP Ribose Transferases / Q000378:metabolism; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D019204:GTP-Binding Proteins / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction
D001427:Bacterial Toxins; D008565:Membrane Proteins; D036002:ADP Ribose Transferases; D019204:GTP-Binding Proteins