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- W1528762007 abstract "Publisher Summary This chapter describes the in vitro ADP-ribosylation of Rho by bacterial ADP-ribosyltransferases. A growing family of intracellularly acting bacterial protein toxins has been characterized by ADP-ribosyltransferase activity. These toxins split NAD into ADP-ribose and nicotinamide and transfer the ADP-ribose moiety onto eukaryotic target proteins. The covalent modification formed is highly selective and causes gross changes in the physiological functions of the target proteins. The toxins are, therefore, of importance not only as bacterial virulence factors but also as tools in cell biology to study the structure and functions of their eukaryotic target proteins. Several bacterial ADP-ribosyltransferases modify small GTPases of the Rho family. Clostridium botulinum ( C . botulinum ) C3 transferase is produced by various strains of C . botulinum types C and D. The transferase selectively modifies the low-molecular-mass GTP-binding proteins RhoA, B, and C, which are involved in the organization and regulation of the actin cytoskeleton." @default.
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- W1528762007 date "1995-01-01" @default.
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- W1528762007 title "[21] In Vitro ADP-ribosylation of Rho by bacterial ADP-ribosyltransferases" @default.
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- W1528762007 doi "https://doi.org/10.1016/0076-6879(95)56023-8" @default.
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