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Article

Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli.

Journal of bacteriology - 1 Jul 1990

Bell P E, Nau C D, Brown J T, Konisky J, Kadner R J

Abstract excerpt

Energy-coupled reactions of the Escherichia coli outer membrane transport proteins BtuB and Cir require the tonB product. Some point mutations in a region of btuB and cir that is highly conserved in TonB-dependent transport proteins led to loss of TonB-coupled uptake of vitamin B12 and colicin Ia, whereas binding was unaffected. Most other point mutations in this region had no detectable effect on transport...

Topics

Alleles
Bacterial Outer Membrane Proteins
Bacterial Proteins
Base Sequence
Biological Transport
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Membrane Proteins
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Oligonucleotide Probes

Suppression, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 2193917
DOI: 10.1128/jb.172.7.3826-3829.1990
PMCID: PMC213362

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2193917-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli.PMID 2193917Read ↗

Molecular characterization of the Enterobacter aerogenes tonB gene: identification of a novel type of tonB box suppressor mutant.Semantic proximity Read ↗

Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.Semantic proximity Read ↗

The wild-type allele of tonB in Escherichia coli is dominant over the tonB1 allele, encoding TonBQ160K, which suppresses the btuB451 mutation.Semantic proximity Read ↗

Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein.Semantic proximity Read ↗

Structure-function analysis of the vitamin B12 receptor of Escherichia coli by means of informational suppression.Semantic proximity Read ↗

Partial suppression of an Escherichia coli TonB transmembrane domain mutation (delta V17) by a missense mutation in ExbB.Semantic proximity Read ↗

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

TonB and the gram-negative dilemma.Semantic proximity Read ↗

Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Semantic proximity Read ↗

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

Performance of standard phenotypic assays for TonB activity, as evaluated by varying the level of functional, wild-type TonB.Semantic proximity Read ↗

Identification of the periplasmic cobalamin-binding protein BtuF of Escherichia coli.Semantic proximity Read ↗

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