Translocation of colicin from the receptor to the inner cell membrane: function of the peptidoglycan layer
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12094727
DOI
10.1007/bf02817640
Knihovny.cz E-resources
- MeSH
- Cell Membrane drug effects metabolism MeSH
- Escherichia coli drug effects genetics metabolism MeSH
- Colicins metabolism pharmacology MeSH
- Membrane Proteins genetics metabolism MeSH
- Peptidoglycan chemistry MeSH
- Escherichia coli Proteins genetics metabolism MeSH
- Spheroplasts drug effects metabolism MeSH
- Protein Transport MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Colicins MeSH
- Membrane Proteins MeSH
- Peptidoglycan MeSH
- Escherichia coli Proteins MeSH
- tolA protein, E coli MeSH Browser
- tolQ protein, E coli MeSH Browser
- tolR protein, E coli MeSH Browser
Sensitivity of spheroplasts (prepared in two ways) of a colicin-sensitive strain, of colicin-resistant and of colicin-tolerant mutants and of strains immune to colicins E1 and E2 was estimated and compared. Generally, the removal of the peptidoglycan layer brought about a slight nonspecific support for colicin translocation across the cell wall in sensitive, tolB tolerant and immune bacteria. tolB spheroplasts were colicin E1-sensitive, but E2-insensitive. Spheroplasts were always fragile and lysed spontaneously, especially those produced by lysozyme. Bacteria carrying tolA, tolQ and tolR mutations kept their colicin insensitivity as spheroplasts, just as the resistant ones. Bacteria rendered colicinogenic and hence colicin-immune turned to high colicin sensitivity in spheroplast form. The results indicate a change in plasma membrane associated with the spheroplast formation.
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