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

Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ.

Journal of bacteriology - 1 Aug 1999

Journet L, Rigal A, Lazdunski C, Bénédetti H

Abstract excerpt

The Tol-PAL system of Escherichia coli is a multiprotein system involved in maintaining the cell envelope integrity and is necessary for the import of some colicins and phage DNA into the bacterium. It is organized into two complexes, one near the outer membrane between TolB and PAL and one in the cytoplasmic membrane between TolA, TolQ, and TolR. In the cytoplasmic membrane, all of the Tol proteins have been...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Colicins
Share to Coliphages

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

Share to Cross-Linking Reagents

Share to Dimerization

Share to Escherichia coli Proteins

Share to Gene Expression Regulation, Bacterial

Share to Peptide Fragments

Source

Open in PubMed Open full text

Identifiers

PMID: 10419942
DOI: 10.1128/JB.181.15.4476-4484.1999
PMCID: PMC103575

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

Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ.PMID 10419942Read ↗

Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins.Semantic proximity Read ↗

Transmembrane alpha-helix interactions are required for the functional assembly of the Escherichia coli Tol complex.Semantic proximity Read ↗

The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB.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 ↗

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 ↗

Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli.Semantic proximity Read ↗

TolA central domain interacts with Escherichia coli porins.Semantic proximity Read ↗

The linker region plays an important role in the interdomain communication of the response regulator OmpR.Semantic proximity Read ↗

Escherichia coli tol-pal mutants form outer membrane vesicles.Semantic proximity Read ↗

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

The Escherichia coli Lpt transenvelope protein complex for lipopolysaccharide export is assembled via conserved structurally homologous domains.Semantic proximity Read ↗

Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins.Semantic proximity Read ↗

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