Abstract
The translocation of protein toxins into a cell relies on a myriad of protein-protein interactions. one such group of toxins are enzymatic E colicins, protein antibiotics produced by Escherichia coli in times of stress. These proteins subvert ordinary nutrient uptake mechanisms to enter the cell and unleash nuclease activity. We, and others, have previously shown that uptake of CoIE9 (colicin E9) is dependent on engagement of the OM (outer membrane) receptors BtuB and OmpF as well as recruitment of the periplasmic protein ToIB, forming a large supramolecular complex. intriguingly, colicins bind ToIB using a natively disordered region to mimic the interaction of ToIB with Pal (pepticloglycan-associated lipoprotein). This is thought to trigger OM instability and prime the system for translocation. Here, we review key interactions in the assembly of this 'colicin translocon' and discuss the key role disorder plays in achieving uptake.
| Original language | English |
|---|---|
| Pages (from-to) | 1409-1413 |
| Number of pages | 5 |
| Journal | Biochemical Society transactions |
| Volume | 36 |
| Issue number | Pt 6 |
| DOIs | |
| Publication status | Published - Dec 2008 |
Keywords
- colicin
- Escherichia coli
- molecular mimicry
- native disorder
- protonmotive force (pmf)
- translocation
- PROTEIN-PROTEIN INTERACTIONS
- C-TERMINAL DOMAIN
- ESCHERICHIA-COLI
- OUTER-MEMBRANE
- COMPETITIVE RECRUITMENT
- CRYSTAL-STRUCTURES
- TOLERANT MUTANTS
- OMPF-PORIN
- TOLB
- E9