Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Biochemical Society transactions - 1 Dec 2012

Lloubès Roland, Goemaere Emilie, Zhang Xiang, Cascales Eric, Duché Denis

Abstract excerpt

Colicins are bacterial toxins that parasitize OM (outer membrane) receptors to bind to the target cells, use an import system to translocate through the cell envelope and then kill sensitive cells. Colicins classified as group A (colicins A, E1-E9, K and N) use the Tol system (TolA, TolB, TolQ and TolR), whereas group B colicins (colicins B, D, Ia, M and 5) use the ExbB-ExbD-TonB system. Genetic evidence has...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Colicins
Share to Escherichia coli Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genetic Complementation Test

Share to Membrane Potentials

Share to Periplasmic Proteins

Share to Protein Interaction Domains and Motifs

Share to Protein Subunits

Share to Protein Transport

Source

Identifiers

PMID: 23176502
DOI: 10.1042/BST20120181

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

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Energetics of colicin import revealed by genetic cross-complementation between the Tol and Ton systems.PMID 23176502Read ↗

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 ↗

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 ↗

Quantification of group A colicin import sites.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 ↗

Energy-dependent immunity protein release during tol-dependent nuclease colicin translocation.Semantic proximity Read ↗

Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA.Semantic proximity Read ↗

Tol-dependent macromolecule import through the Escherichia coli cell envelope requires the presence of an exposed TolA binding motif.Semantic proximity Read ↗

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

Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains.Semantic proximity Read ↗

Specific TonB-ExbB-ExbD energy transduction systems required for ferric enterobactin acquisition in Campylobacter.Semantic proximity Read ↗

Mutations in enterobacterial common antigen biosynthesis restore outer membrane barrier function in Escherichia coli tol-pal mutants.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.