Document Detail


Identification of Glu173 as the critical amino acid residue for the ADP-ribosyltransferase activity of Clostridium botulinum C3 exoenzyme.
MedLine Citation:
PMID:  7672106     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Y Saito; Y Nemoto; T Ishizaki; N Watanabe; N Morii; S Narumiya
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  371     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1995 Sep 
Date Detail:
Created Date:  1995-10-16     Completed Date:  1995-10-16     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  105-9     Citation Subset:  IM    
Affiliation:
Department of Pharmacology, Kyoto University Faculty of Medicine, Japan.
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
ADP Ribose Transferases / chemistry*,  genetics,  metabolism*
Animals
Base Sequence
Binding Sites
Botulinum Toxins*
Glutamic Acid*
Mice
Molecular Sequence Data
Mutagenesis, Site-Directed
NAD / metabolism
Poly(ADP-ribose) Polymerases / metabolism*
Structure-Activity Relationship
Tryptophan
Chemical
Reg. No./Substance:
0/Botulinum Toxins; 53-84-9/NAD; 56-86-0/Glutamic Acid; 73-22-3/Tryptophan; EC 2.4.2.-/ADP Ribose Transferases; EC 2.4.2.-/exoenzyme C3, Clostridium botulinum; EC 2.4.2.30/Poly(ADP-ribose) Polymerases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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