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ADP-Ribosylation of Small GTPases by Clostridium botulinum Exoenzyme C3 and Pseudomonas aeruginosa Exoenzyme S

  • Chapter
GTPases in Biology I

Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 108 / 1))

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Abstract

Bacterial toxins have served as important tools for the study of eukaryotic cell biology, especially signal transduction by the heterotrimeric G-proteins. Many of these toxins catalyze the ADP-ribosylation of specific proteins inside the host cell. In this reaction, the nicotinamide-ribose bond of nicotinamide-adenine dinucleotide (NAD) is split and the ADP-ribose moiety is transferred to the substrate protein. Most of these toxins, termed ADP-ribosyltransferases, modify G-proteins or other GTPases. The addition of the ADP-ribose group to the substrate protein alters the function of that protein dramatically. For example, ADP-ribosylation of Gsα by cholera toxin decreases GTP hydrolysis (Cassel and Selinger 1977), while the modification of Giα by pertussis toxin alters its interaction with receptors (Kurose et al. 1983; Murayama and Ui 1983). Diphtheria toxin and Pseudomonas exotoxin A both ADP-ribosylate the same residue in elongation factor 2 (EF-2), and inhibit interaction of EF-2 with the ribosome (Collier 1967; Iglewski and Kabat 1975). In all cases, the actions of the toxins on the GTPases have drastic consequences for the eukaryotic cell, as normal signal transduction is disrupted. An additional characteristic of the bacterial ADP-ribosyltransferases is that they all have well-defined cell-binding or “B” components that are functionally distinct from the “A” domains, which are enzymically active after entry into the cytosol.

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Authors
  1. J. Coburn
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Editors and Affiliations

  1. Department of Medicine, Cell Biology and Experimental Therapeutics, Room 3C-385, Houston VA Medical Center, Baylor College of Medicine, 2002 Holcombe Boulevard, Houston, TX, 77030, USA

    Burton F. Dickey M.D.

  2. Department of Cell Biology, Molecular Physiology and Biophysics, Medicine and Neurosciences, Baylor College of Medicine, One Baylor Plaza, Houston, TX, 77030, USA

    Lutz Birnbaumer Ph.D.

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© 1993 Springer-Verlag Berlin Heidelberg

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Coburn, J. (1993). ADP-Ribosylation of Small GTPases by Clostridium botulinum Exoenzyme C3 and Pseudomonas aeruginosa Exoenzyme S. In: Dickey, B.F., Birnbaumer, L. (eds) GTPases in Biology I. Handbook of Experimental Pharmacology, vol 108 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78267-1_43

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  • DOI: https://doi.org/10.1007/978-3-642-78267-1_43

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-78269-5

  • Online ISBN: 978-3-642-78267-1

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