Novel approaches to the mode of action of colicins
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, přehledy
PubMed
1095464
DOI
10.1007/bf02876789
Knihovny.cz E-zdroje
- MeSH
- antibiotická rezistence MeSH
- Bacteria účinky léků metabolismus MeSH
- bakteriální proteiny biosyntéza MeSH
- biologické modely MeSH
- buněčná membrána fyziologie MeSH
- buněčná stěna metabolismus MeSH
- denaturace nukleových kyselin MeSH
- Escherichia coli účinky léků fyziologie MeSH
- kinetika MeSH
- koliciny analýza metabolismus farmakologie MeSH
- L-formy bakterií metabolismus MeSH
- mutace MeSH
- nukleové kyseliny metabolismus MeSH
- receptory léků * MeSH
- tolerance léku MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- bakteriální proteiny MeSH
- koliciny MeSH
- nukleové kyseliny MeSH
- receptory léků * MeSH
According to the theory of Fredericq (1949) and Nomura (1964), colicins are attached by specific receptor sites in the cell walls of sensitive bacteria, which mediate their inhibitive effects. During last years, a great variety of experimental data have been accumulated, some of which cannot be easily interpreted in terms of this theory. There exist considerable discrepancies concerning the chemical nature and molecular weight of isolated receptors. The attachment of a colicin onto its receptor need not be irreversible. The inhibition of numerous membrane-associated functions in colicin-tolerant mutants suggests their pleiotropic deletion nature. The difference between colicin resistance and colicin tolerance does not seem to be clear-cut. Cells of stable L-forms of protoplast type, completely devoid of their walls, retain in most cases the same patterns of sensitivity to colicins as rods of the same strains. Experimental changes in the relationship between the cell wall and the cytoplasmic membrane decrease colicin sensitivity of the cells. Colicin E3 has been found to be a specific endoribonuclease, able to cleave a terminal fragment from the 16 S rRNA also in isolated ribosomes in vitro: not only in ribosomes from sensitive bacteria, but also in those from resistant ones and from eukaryotic cells. A destabilization of the DNA helix was induced by colicin E2 in vitro as in vivo. It seems that there exist two distinct types of colicin receptors with different functions: those in the cell wall, and those in the cytoplasmic membrane. Only the contact of colicins with the latter ones is biologically effective and starts both stages of their inhibitive effect: the reversible and the irreversible ones.
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Colicins--exocellular lethal proteins of Escherichia coli