Titlebook: Bacteriocins, Microcins and Lantibiotics; Richard James,Claude Lazdunski,Franc Pattus Conference proceedings 1992 Springer-Verlag Berlin H

colloquial

Pore Forming Bacteriocinsvent within the core of a compact globular protein. Presumably, the other pore-forming colicins have a similar structure. Despite our knowledge of this structure, however, the mechanism of membrane insertion, of channel induction by membrane potential, and the structure of the channel itself are sti

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, Properties of Colicin A: Channel Activity and Translocation, the primary effects of these colicins are a leakage of cytoplasmic K. (Wendt, 1970) and small ions (Lusk and Nelson, 1972), a decrease of internal ATP, a collapse of the electrochemical gradient of protons (Δ μH .), and consequently an inhibition of the ΔμH.-driven active transport systems (for re

战役

Site-Directed Fluorescence Spectroscopy as a Tool to Study the Membrane Insertion of Colicin Aesis via the . gene, various processes occur which allow the protein to pass into the ambient medium.The plasmid-carrying cells are resistant to the effects of their own toxin due to the presence on the same plasmid of the . gene which codes for the “immunity protein”. These features will be fully d

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Immunity Protein to Pore Forming Colicins mutations in genes encoding proteins involved in their entry into bacteria render the cells insensitive to their action. These mechanisms of insensitivity are not highly specific to the action of a particular colicin since many colicins share common components in their uptake system (see the Chapte

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Specificity Determinants of the Interaction Between Colicin E9 and its Immunity ProteiniMasi et al., 1973). Each E colicin plasmid also codes for the production of a specific immunity protein which, on synthesis, binds to the C-terminal domain of its cognate colicin (with the exception of the colicin El immunity protein). This is assumed to protect the producing . cells from being kil

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