Purification of TAT-C3 exoenzyme

Sahai, E. and Olson, M. (2006) Purification of TAT-C3 exoenzyme. Methods in Enzymology, 406, pp. 128-140. (doi: 10.1016/S0076-6879(06)06011-3)

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Abstract

The Clostridium botulinum C3 exoenzyme has been an invaluable tool for the study of the biological functions of Rho GTPases. The C3 enzyme selectively catalyzes the ADP-ribosylation, and consequent inactivation, of RhoA, RhoB, and RhoC of the Rho GTPase protein family. Through the experimental use of C3, it has been possible to determine the contributions made by these signaling proteins to processes including the regulation of cell morphology, cell cycle progression, and gene transcription. Unlike bacterial toxins that have some means to attach to and/or enter cells, C3 does not have an element that facilitates efficient entry. As a result, numerous methods have been used to effectively deliver C3 into cells. One approach has been to engineer a recombinant C3 with an HIV TAT leader sequence that permits transduction of the protein across the plasma membrane. In this chapter, the purification and characterization of the recombinant TAT-C3 protein is described.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Olson, Professor Michael
Authors: Sahai, E., and Olson, M.
College/School:College of Medical Veterinary and Life Sciences > School of Cancer Sciences
Journal Name:Methods in Enzymology
ISSN:0076-6879
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