Identification of Glu173as the critical amino acid residue for the ADP-ribosyltransferase activity ofClostridium botulinumC3 exoenzyme
Open Access
- 4 September 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 371 (2) , 105-109
- https://doi.org/10.1016/0014-5793(95)00851-y
Abstract
Clostridium botulinum C3 exoenzyme specifically ADP‐ribosylates rho‐p21 in eukaryotic cells. Trp18 and Glu173 of this enzyme were substituted with other amino acids via site‐directed mutagenesis. All substitutions at Glu173 caused a significant reduction in affinity for NAD and diminished ADP‐ribosyltransferase activity. On the other hand, the activity of enzymes with the substitution at Trp18 remained intact. Swiss 3T3 cells treated with the enzyme with the Trp18 substitution showed the typical morphologic changes of the C3 exoenzyme phenotype. In contrast, no changes were found in cells incubated with the Glu173‐substituted enzyme. These results indicate that the Glu173 residue of the C3 exoenzyme plays a key role in interacting with NAD and in expression of ADP‐ribosyltransferase activity, which is essential for the phenotypic change by C3 exoenzyme treatment.Keywords
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