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Updated: Aug 22, 2026

An In Vitro Assay to Detect tRNA-Isopentenyl Transferase Activity
Published on: October 8, 2018
Rho-modifying C3-like ADP-ribosyltransferases
K Aktories1, C Wilde, M Vogelsgesang
1Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University Freiburg, Otto-Krayer-Haus, Albertstr. 25, Freiburg, Germany. Klaus.Aktories@pharmakol.uni-freiburg.de.
Abstract:
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 are established pharmacological tools to study the cellular functions of Rho GTPases. Recent studies, however, indicate that the functional consequences of C3-induced ADP-ribosylation are more complex than previously suggested. In the present review the basic properties of C3 exoenzymes are briefly summarized and new findings are reviewed.
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