The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli

Bradbeer, C

doi:10.1128/jb.175.10.3146-3150.1993

Cited by 188Bacterial Genetics and BiotechnologyDrug Transport and Resistance MechanismsATP Synthase and ATPases Research

The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli

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Bradbeer, C·1993·Journal of Bacteriology

DOI 10.1128/jb.175.10.3146-3150.1993PMC PMC204637

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Abstract

Cells of Escherichia coli pump cobalamin (vitamin B12) across their outer membranes into the periplasmic space, and it was concluded previously that this process is potentiated by the proton motive force of the inner membrane. The novelty of such an energy coupling mechanism and its relevance to other outer membrane transport processes have required confirmation of this conclusion by studies with cells in which cobalamin transport is limited to the outer membrane. Accordingly, I have examined the effects of cyanide and of 2,4-dinitrophenol on cobalamin uptake in btuC and atp mutants, which lack inner membrane cobalamin transport and the membrane-bound ATP synthase, respectively. Dinitrophenol eliminated cobalamin transport in all strains, but cyanide inhibited this process only in atp and btuC atp mutant cells, providing conclusive evidence that cobalamin transport across the outer membrane requires specifically the proton motive force of the inner membrane. The coupling of metabolic energy to outer membrane cobalamin transport requires the TonB protein and is stimulated by the ExbB protein. I show here that the tolQ gene product can partly replace the function of the ExbB protein. Cells with mutations in both exbB and tolQ had no measurable cobalamin transport and thus had a phenotype that was essentially the same as TonB-. I conclude that the ExbB protein is a normal component of the energy coupling system for the transport of cobalamin across the outer membrane.

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Self-citation
Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity
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Authors: Bradbeer, C.
Affiliations: University of Virginia (US)
Corresponding author: Bradbeer, C
Venue: Journal of Bacteriology
Publisher: American Society for Microbiology
Published: 1993-05
Volume: 175
Issue: 10
Pages: 3146-3150
ISSN: 0021-9193 (ISSN-L)
1098-5530
DOI: 10.1128/jb.175.10.3146-3150.1993
PMC: PMC204637
OpenAlex: W1912992879
Cited by: 188
References: 26
Citations by year: 2026: 3 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 8 · 2020: 3 · 2019: 3 · 2018: 1 · 2017: 2 · 2016: 6 · 2015: 3 · 2014: 6 · 2013: 7 · 2012: 4
FWCI: 4.84
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Journal of Bacteriology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: cobalamin uptake, vitamin B12, outer membrane transport, proton motive force, Escherichia coli, TonB, ExbB, TolQ, 2,4-dinitrophenol, cyanide, energy coupling, periplasmic transport
MeSH terms: Bacterial Proteins, Biological Transport, Active, Cell Membrane, Cyanides, Dinitrophenols, Escherichia coli, Proton-Translocating ATPases, Membrane Proteins, Protons, Transduction, Genetic, Vitamin B 12, Mutagenesis, ATP-Binding Cassette Transporters, 2,4-Dinitrophenol, Escherichia coli Proteins

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The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli

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