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Article

Quantification of group A colicin import sites.

Journal of bacteriology - 1 Sept 1995

Duché D, Letellier L, Géli V, Bénédetti H, Baty D

Abstract excerpt

Pore-forming colicins are soluble bacteriocins which form voltage-gated ion channels in the inner membrane of Escherichia coli. To reach their target, these colicins first bind to a receptor located on the outer membrane and then are translocated through the envelope. Colicins are subdivided into two groups according to the envelope proteins involved in their translocation: group A colicins use the Tol proteins;...

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Source

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Identifiers

PMID: 7545150
DOI: 10.1128/jb.177.17.4935-4939.1995
PMCID: PMC177268

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Quantification of group A colicin import sites.PMID 7545150Read ↗

Energetics of colicin import revealed by genetic cross-complementation between the Tol and Ton systems.Semantic proximity Read ↗

Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli.Semantic proximity Read ↗

The TolA-recognition site of colicin N. ITC, SPR and stopped-flow fluorescence define a crucial 27-residue segment.Semantic proximity Read ↗

Protein import into Escherichia coli: colicins A and E1 interact with a component of their translocation system.Semantic proximity Read ↗

Import-defective colicin B derivatives mutated in the TonB box.Semantic proximity Read ↗

TonB system, in vivo assays and characterization.Semantic proximity Read ↗

Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering.Semantic proximity Read ↗

Characterization of colicin S4 and its receptor, OmpW, a minor protein of the Escherichia coli outer membrane.Semantic proximity Read ↗

Gating movements of colicin A and colicin Ia are different.Semantic proximity Read ↗

Novel colicin 10: assignment of four domains to TonB- and TolC-dependent uptake via the Tsx receptor and to pore formation.Semantic proximity Read ↗

Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9.Semantic proximity Read ↗

Membrane topology of the colicin E1 channel using genetically encoded fluorescence.Semantic proximity Read ↗

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