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Article

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

Journal of molecular biology - 10 Feb 1995

Lazzaroni J C, Vianney A, Popot J L, Bénédetti H, Samatey F, Lazdunski C, Portalier R, Géli V

Abstract excerpt

TolQ, TolR and TolA are membrane proteins involved in maintaining the structure of Escherichia coli cell envelope. TolQ and TolR span the inner membrane with three and with one alpha-helical segments, respectively. The tolQ925 mutation (A177V), located in the third putative transmembrane helix of TolQ (TolQ-III), induces cell sensitivity to bile salts and tolerance towards colicin A but not colicin E1, unlike a...

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Identifiers

PMID: 7853390
DOI: 10.1006/jmbi.1994.0058

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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.

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Transmembrane alpha-helix interactions are required for the functional assembly of the Escherichia coli Tol complex.PMID 7853390Read ↗

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

Escherichia coli TolA tolerates multiple amino-acid substitutions as revealed by screening randomized variants for membrane integrity and phage receptor function.Semantic proximity Read ↗

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

The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB.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 TolC protein of Escherichia coli serves as a cell-surface receptor for the newly characterized TLS bacteriophage.Semantic proximity Read ↗

Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution.Semantic proximity Read ↗

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

Recombineering with tolC as a selectable/counter-selectable marker: remodeling the rRNA operons of Escherichia coli.Semantic proximity Read ↗

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

The Lack of the Essential LptC Protein in the Trans-Envelope Lipopolysaccharide Transport Machine Is Circumvented by Suppressor Mutations in LptF, an Inner Membrane Component of the Escherichia coli Transporter.Semantic proximity Read ↗

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