Copurification of rho protein and the rho-GDP dissociation inhibitor from bovine neutrophil cytosol. Effect of phosphoinositides on rho ADP-ribosylation by the C3 exoenzyme of Clostridium botulinum

Biochemistry ◽  
1992 ◽  
Vol 31 (51) ◽  
pp. 12863-12869 ◽  
Author(s):  
Nicolas Bourmeyster ◽  
Marie Jose Stasia ◽  
Jerome Garin ◽  
Jean Gagnon ◽  
Patrice Boquet ◽  
...  
Keyword(s):  
Clostridium Botulinum ◽  
Adp Ribosylation ◽  
Rho Protein ◽  
C3 Exoenzyme ◽  
Gdp Dissociation Inhibitor ◽  
Bovine Neutrophil

ADP-ribosylation of a small size GTP-binding protein in bovine neutrophils by the C3 exoenzyme of Clostridium botulinum and effect on the cell motility

1991 ◽  
Vol 180 (2) ◽  
pp. 615-622 ◽  
Author(s):  
Marie-Jose Stasia ◽  
Alain Jouan ◽  
Nicolas Bourmeyster ◽  
Patrice Boquet ◽  
Pierre V. Vignais
Keyword(s):  
Cell Motility ◽  
Clostridium Botulinum ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Adp Ribosylation ◽  
Gtp Binding ◽  
C3 Exoenzyme ◽  
Bovine Neutrophils

scholarly journals Differentiation-induced increase in Clostridium botulinum C3 exoenzyme-catalyzed ADP-ribosylation of the small GTP-binding protein Rho

1994 ◽  
Vol 223 (3) ◽  
pp. 909-916 ◽  
Author(s):  
Gerhard FRITZ ◽  
Ingo JUST ◽  
Peter WOLLENBERG ◽  
Klaus AKTORIES
Keyword(s):  
Clostridium Botulinum ◽  
Binding Protein ◽  
Gtp Binding Protein ◽  
Adp Ribosylation ◽  
Gtp Binding ◽  
C3 Exoenzyme

Activation of Clostridium botulinum C3 Exoenzyme-Catalyzed ADP-Ribosylation of RhoA by K+in a Mg2+-Dependent Manner

1996 ◽  
Vol 119 (1) ◽  
pp. 200-207 ◽  
Author(s):  
T. Miyaoka ◽  
M. Tsuchiya ◽  
N. Hara ◽  
H. Ishino ◽  
M. Shimoyama
Keyword(s):  
Clostridium Botulinum ◽  
Dependent Manner ◽  
Adp Ribosylation ◽  
C3 Exoenzyme

scholarly journals ADP-ribosylation by Clostridium botulinum C3 exoenzyme increases steady-state GTPase activities of recombinant rhoA and rhoB proteins

FEBS Letters ◽  
1992 ◽  
Vol 297 (1-2) ◽  
pp. 95-99 ◽  
Author(s):  
Christiane Mohr ◽  
Gertrud Koch ◽  
Ingo Just ◽  
Klaus Aktories
Keyword(s):  
Steady State ◽  
Clostridium Botulinum ◽  
Adp Ribosylation ◽  
C3 Exoenzyme

scholarly journals Synergistic Activation of Rat Brain Phospholipase D by ADP-ribosylation Factor and rhoA p21, and Its Inhibition by Clostridium botulinum C3 Exoenzyme

1995 ◽  
Vol 270 (43) ◽  
pp. 25667-25671 ◽  
Author(s):  
Hideo Kuribara ◽  
Kenji Tago ◽  
Takeaki Yokozeki ◽  
Takuya Sasaki ◽  
Yoshimi Takai ◽  
...  
Keyword(s):  
Rat Brain ◽  
Phospholipase D ◽  
Clostridium Botulinum ◽  
Adp Ribosylation ◽  
Synergistic Activation ◽  
C3 Exoenzyme ◽  
Adp Ribosylation Factor

scholarly journals ADP-ribosylation of actin isoforms by Clostridium botulinum C2 toxin and Clostridium perfringens iota toxin

1990 ◽  
Vol 194 (1) ◽  
pp. 237-241 ◽  
Author(s):  
Stefan MAUSS ◽  
Christine CHAPONNIER ◽  
Ingo JUST ◽  
Klaus AKTORIES ◽  
Giulio GABBIANI
Keyword(s):  
Clostridium Perfringens ◽  
Clostridium Botulinum ◽  
Actin Isoforms ◽  
Adp Ribosylation ◽  
Clostridium Botulinum C2 Toxin ◽  
Clostridium Perfringens Iota Toxin ◽  
C2 Toxin

Clostridium botulinum C3 Exoenzyme and Studies on Rho Proteins

2008 ◽  
pp. 71-83 ◽  
Author(s):  
C. D. Nobes ◽  
A. Hall
Keyword(s):  
Clostridium Botulinum ◽  
Rho Proteins ◽  
C3 Exoenzyme

scholarly journals ADP-Ribosylation of Actin by the Clostridium botulinum C2 Toxin in Mammalian Cells Results in Delayed Caspase-Dependent Apoptotic Cell Death

2008 ◽  
Vol 76 (10) ◽  
pp. 4600-4608 ◽  
Author(s):  
Karin Heine ◽  
Sascha Pust ◽  
Stefanie Enzenmüller ◽  
Holger Barth
Keyword(s):  
Cell Death ◽  
Cell Lines ◽  
Mammalian Cells ◽  
Clostridium Botulinum ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Adp Ribosylation ◽  
Mammalian Cell Lines ◽  
Adp Ribosyltransferase ◽  
C2 Toxin

ABSTRACT The binary C2 toxin from Clostridium botulinum mono-ADP-ribosylates G-actin in the cytosol of eukaryotic cells. This modification leads to depolymerization of actin filaments accompanied by cell rounding within 3 h of incubation but does not immediately induce cell death. Here we investigated the long-term responses of mammalian cell lines (HeLa and Vero) following C2 toxin treatment. Cells stayed round even though the toxin was removed from the medium after its internalization into the cells. No unmodified actin reappeared in the C2 toxin-treated cells within 48 h. Despite actin being completely ADP-ribosylated after about 7 h, no obvious decrease in the overall amount of actin was observed for at least 48 h. Therefore, ADP-ribosylation was not a signal for an accelerated degradation of actin in the tested cell lines. C2 toxin treatment resulted in delayed apoptotic cell death that became detectable about 15 to 24 h after toxin application in a portion of the cells. Poly(ADP)-ribosyltransferase 1 (PARP-1) was cleaved in C2 toxin-treated cells, an indication of caspase 3 activation and a hallmark of apoptosis. Furthermore, specific caspase inhibitors prevented C2 toxin-induced apoptosis, implying that caspases 8 and 9 were activated in C2 toxin-treated cells. C2I, the ADP-ribosyltransferase component of the C2 toxin, remained active in the cytosol for at least 48 h, and no extensive degradation of C2I was observed. From our data, we conclude that the long-lived nature of C2I in the host cell cytosol was essential for the nonreversible cytotoxic effect of C2 toxin, resulting in delayed apoptosis of the tested mammalian cells.

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