Colicin D: Difference between revisions
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==Mechanism of uptake== | ==Mechanism of uptake== | ||
The receptor binding domain of the colicin binds to the outer membrane receptor FepA on the target cell; it is a constitutively expressed protein parasitised by the colicin. The translocation domain then recruits proteins from the [[Ton]] system to translocate the protein across the membrane and into the cytoplasm. | |||
==Killing Activities== | ==Killing Activities== | ||
Revision as of 22:04, 25 March 2011
Colicin D is a type of Colicin, a bacteriocin made by E. coli which acts against other nearby E. coli to kill them with its tRNase activity; it digests specific tRNAs, inhibiting protein synthesis and leading to the death of the cell.
Synthesis and releaseSynthesis and release
The operon for colicin D is encoded on a plasmid in the cytoplasm of the E. coli. This operon also encodes its Colicin Immunity Protein, ImmD, to protect the membrane of the cell from the tRNase activities of the colicin, alongside a protein to aid the release of the colicin outside the cell.
Once produced, the immunity protein binds to the cytotoxic domain of the colicin and inhibits its enzymatic activity.
Mechanism of uptakeMechanism of uptake
The receptor binding domain of the colicin binds to the outer membrane receptor FepA on the target cell; it is a constitutively expressed protein parasitised by the colicin. The translocation domain then recruits proteins from the Ton system to translocate the protein across the membrane and into the cytoplasm.