| Autor: |
Dagmar Blöcker, Kathrin Pohlmann, Christoph Bachmeyer, Gerd Haug, Klaus Aktories, Holger Barth, Roland Benz |
| Rok vydání: |
2003 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 278:37360-37367 |
| ISSN: |
0021-9258 |
| DOI: |
10.1074/jbc.m305849200 |
| Popis: |
The binary Clostridium botulinum C2 toxin consists of two individual proteins, the transport component C2II (80 kDa) and the enzyme component C2I, which ADP-ribosylates G-actin in the cytosol of cells. Trypsin-activated C2II (C2IIa) forms heptamers that bind to the cell receptor and mediate translocation of C2I from acidic endosomes into the cytosol of target cells. Here, we report that translocation of C2I across cell membranes is accompanied by pore formation of C2IIa. We used a radioactive rubidium release assay to detect C2IIa pores in the membranes of Chinese hamster ovary cells. Pore formation by C2IIa was dependent on the cellular C2 toxin receptor and an acidic pulse. Pores were formed when C2IIa was bound to cells at neutral pH and when cells were subsequently shifted to acidic medium (pH |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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