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C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins - PubMed

Review

. 2007 Feb;374(5-6):347-60.

doi: 10.1007/s00210-006-0113-y. Epub 2006 Dec 5.

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Review

C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins

Martin Vogelsgesang et al. Naunyn Schmiedebergs Arch Pharmacol. 2007 Feb.

Abstract

The family of C3-like exoenzymes comprises seven bacterial ADP-ribosyltransferases of different origin. The common hallmark of these exoenzymes is the selective N-ADP-ribosylation of the low molecular mass GTP-binding proteins RhoA, B, and C and inhibition of signal pathways controlled by Rho GTPases. Therefore, C3-like exoenzymes were applied as pharmacological tools for analyses of cellular functions of Rho protein in numerous studies. Recent structural and functional analyses of C3-like exoenzymes provide detailed information on the molecular mechanisms and functional consequences of ADP-ribosylation catalyzed by these toxins. More recently additional non-enzymatic actions of C3-like ADP-ribosyltransferases have been identified showing that C3 transferases from Clostridium botulinum and Clostridium limosum form a GDI-like complex with the Ras-like low molecular mass GTPase Ral without ADP-ribosylation. These results add novel information on the molecular mode of action(s) of C3-like exoenzymes and are discussed in this review.

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