Journal article
Topographic analysis of the toxic Gef protein from Escherichia coli
The chromosomal gef gene of Escherichia coli is a member of the gef gene family which encodes strongly toxic proteins of about 50 amino acids. We demonstrate here that the Gef protein is detectable by anti-peptide antibodies. Furthermore, we show that Gef is anchored in the cytoplasmic membrane by the N-terminal part of the protein, and that the C-terminal part is localized in the periplasm in a dimeric form with at least one disulphide bond.
By mutagenesis of gef it is shown that the periplasmic portion of Gef encodes the toxic domain and that the dimerization of Gef is not essential for the toxic effect.
| Language: | English |
|---|---|
| Year: | 1991 |
| Pages: | 1627-1637 |
| ISSN: | 13652958 and 0950382x |
| Types: | Journal article |
| DOI: | 10.1111/j.1365-2958.1991.tb01910.x |
Amino Acid Sequence Bacterial Proteins Bacterial Toxins Base Sequence Blotting, Western Cell Membrane DNA Mutational Analysis Escherichia coli Escherichia coli Proteins Gene Expression Genes, Bacterial HokC protein, E coli Macromolecular Substances Membrane Proteins Molecular Sequence Data Multigene Family Mutagenesis, Site-Directed Plasmids Protein Conformation
