Colicin A and the Tol proteins involved in its translocation are preferentially located in the contact sites between the inner and outer membranes of Escherichia coli cells.

Abstract : Colicin A is a bacterial toxin which forms channels in the cytoplasmic membrane of Escherichia coli. Its translocation through the envelope requires the participation of bacterial proteins encoded by the tolQ, -R, -A, and -B genes. Overproduction of the Tol proteins decreased the time needed for colicin A translocation and increased the number of channels formed in vivo. Cells overproducing radioactively labeled Tol proteins and containing or not colicin A were fractionated. The Tol proteins were mainly recovered in the inner membrane and in the contact sites between the two membranes. The presence of colicin A increased the specific radioactivity of the Tol proteins in the contact sites. Our data suggest that the Tol proteins form a complex of definite stoichiometry in the membranes and that colicin A is associated to this complex upon channel formation. We discuss the possibility that the channel activity determined in vivo is due to the colicin A-Tol proteins complex.
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https://hal.archives-ouvertes.fr/hal-02130218
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Submitted on : Wednesday, May 15, 2019 - 4:26:08 PM
Last modification on : Thursday, May 16, 2019 - 1:37:59 AM

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  • HAL Id : hal-02130218, version 1
  • PUBMED : 8119930

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G. Guihard, P. Boulanger, H Bénédetti, R Lloubés, M Besnard, et al.. Colicin A and the Tol proteins involved in its translocation are preferentially located in the contact sites between the inner and outer membranes of Escherichia coli cells.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1994, 269 (8), pp.5874-80. ⟨hal-02130218⟩

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