Interaction of the Rho-ADP-ribosylating C3 Exoenzyme with RalA

Interaction of the Rho-ADP-ribosylating C3 exoenzyme with RalA.

RhoA, -B, and -C are ADP-ribosylated and biologically inactivated by Clostridium botulinum C3 exoenzyme and related C3-like transferases. We report that RalA GTPase, which is not ADP-ribosylated by C3, inhibits ADP-ribosylation of RhoA by C3 from C. botulinum (C3bot), Clostridium limosum (C3lim), and Bacillus cereus (C3cer) but not from Staphylococcus aureus (C3stau) in human platelet membranes...

The Rho ADP-ribosylating C3 exoenzyme binds cells via an Arg–Gly–Asp motif

The Rho ADP-ribosylating C3 exoenzyme (C3bot) is a bacterial protein toxin devoid of a cell-binding or -translocation domain. Nevertheless, C3 can efficiently enter intact cells, including neurons, but the mechanism of C3 binding and uptake is not yet understood. Previously, we identified the intermediate filament vimentin as an extracellular membranous interaction partner of C3. However, uptak...

Structural basis of Rho GTPase recognition by C3 exoenzyme

C3 exoenzyme is a mono-ADPribosyltransferase (ART) that catalyzes transfer of an ADP-ribose moiety from NAD to Rho GTPases. C3 has long been used to study the diverse regulatory functions of Rho GTPases. How C3 recognizes its substrate and ADP-ribosylation proceeds are still poorly understood. Crystal structures of C3-RhoA complex reveal that C3 recognizes RhoA via switch I, switch II and inter...

Rho-modifying C3-like ADP-ribosyltransferases.

C3-like exoenzymes comprise a family of seven bacterial ADP-ribosyltransferases, which selectively modify RhoA, B, and C at asparagine-41. Crystal structures of C3 exoenzymes are available, allowing novel insights into the structure-function relationships of these exoenzymes. Because ADP-ribosylation specifically inhibits the biological functions of the low-molecular mass GTPases, C3 exoenzymes...

The ADP-Ribosylating CTA1-DD Adjuvant