Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm.

Abstract : Several proteins of the Tol/Pal system are required for group A colicin import into Escherichia coli. Colicin A interacts with TolA and TolB via distinct regions of its N-terminal domain. Both interactions are required for colicin translocation. Using in vivo and in vitro approaches, we show in this study that colicin A also interacts with a third component of the Tol/Pal system required for colicin import, TolR. This interaction is specific to colicins dependent on TolR for their translocation, strongly suggesting a direct involvement of the interaction in the colicin translocation step. TolR is anchored to the inner membrane by a single transmembrane segment and protrudes into the periplasm. The interaction involves part of the periplasmic domain of TolR and a small region of the colicin A N-terminal domain. This region and the other regions responsible for the interaction with TolA and TolB have been mapped precisely within the colicin A N-terminal domain and appear to be arranged linearly in the colicin sequence. Multiple contacts with periplasmic-exposed Tol proteins are therefore a general principle required for group A colicin translocation.
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Journal articles
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https://hal.archives-ouvertes.fr/hal-02130124
Contributor : Laëtitia Legoupil <>
Submitted on : Wednesday, May 15, 2019 - 3:35:54 PM
Last modification on : Thursday, May 16, 2019 - 1:37:55 AM

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  • HAL Id : hal-02130124, version 1
  • PUBMED : 11703658

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L. Journet, E. Bouveret, A. Rigal, R Lloubes, C Lazdunski, et al.. Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm.. Molecular Microbiology, Wiley, 2001, 42 (2), pp.331-44. ⟨hal-02130124⟩

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