Translocation of colicin from the receptor to the inner cell membrane: function of the peptidoglycan layer
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12094727
DOI
10.1007/bf02817640
Knihovny.cz E-zdroje
- MeSH
- buněčná membrána účinky léků metabolismus MeSH
- Escherichia coli účinky léků genetika metabolismus MeSH
- koliciny metabolismus farmakologie MeSH
- membránové proteiny genetika metabolismus MeSH
- peptidoglykan chemie MeSH
- proteiny z Escherichia coli genetika metabolismus MeSH
- sféroplasty účinky léků metabolismus MeSH
- transport proteinů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- koliciny MeSH
- membránové proteiny MeSH
- peptidoglykan MeSH
- proteiny z Escherichia coli MeSH
- tolA protein, E coli MeSH Prohlížeč
- tolQ protein, E coli MeSH Prohlížeč
- tolR protein, E coli MeSH Prohlížeč
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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