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

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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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Additional file 3 of Investigation of the impact of a broad range of temperatures on the physiological and transcriptional profiles of Zymomonas mobilis ZM4 for high-temperature-tolerant recombinant strain development
Li, R., Shen, W., Yang, Y., Du, J., Li, M., & Yang, S. (2021) · Figshare · doi:10.6084/m9.figshare.14863499
Additional file 1 of Investigation of the impact of a broad range of temperatures on the physiological and transcriptional profiles of Zymomonas mobilis ZM4 for high-temperature-tolerant recombinant strain development
Li, R., Shen, W., Yang, Y., Du, J., Li, M., & Yang, S. (2021) · Figshare · doi:10.6084/m9.figshare.14863493
Additional file 4 of Investigation of the impact of a broad range of temperatures on the physiological and transcriptional profiles of Zymomonas mobilis ZM4 for high-temperature-tolerant recombinant strain development
Li, R., Shen, W., Yang, Y., Du, J., Li, M., & Yang, S. (2021) · Figshare · doi:10.6084/m9.figshare.14863502
Additional file 5 of Investigation of the impact of a broad range of temperatures on the physiological and transcriptional profiles of Zymomonas mobilis ZM4 for high-temperature-tolerant recombinant strain development
Li, R., Shen, W., Yang, Y., Du, J., Li, M., & Yang, S. (2021) · Figshare · doi:10.6084/m9.figshare.14863505
Additional file 2 of Investigation of the impact of a broad range of temperatures on the physiological and transcriptional profiles of Zymomonas mobilis ZM4 for high-temperature-tolerant recombinant strain development
Li, R., Shen, W., Yang, Y., Du, J., Li, M., & Yang, S. (2021) · Figshare · doi:10.6084/m9.figshare.14863496
Organisation fonctionnelle des segments transmembranaires d'un moteur moléculaire Tol et d'une protéine active conte une toxine bactérienne
Zhang, X. (2010) · theses.fr (ABES) · doi:10.70675/d27d16e8z4525z4a79z8873z4aea0a491755
Phylogenomic and metabolic insights into iron reduction metabolism in the genus Deferribacter belonging to the order Deferribacterales
Pouder, E., Alain, K., & Mieszkin, S. (2026) · Microbial Genomics · doi:10.1099/mgen.0.001712
Multiple TonB-dependent transport systems in Helicobacter pylori
Loh, J. T., Okoye, C. D., Kunkle, D. E., McDonald, W. H., McClain, M. S., Skaar, E. P., & Cover, T. L. (2026) · Infection and Immunity · doi:10.1128/iai.00018-26
Evidence for a direct link between the Tol-Pal protein complex and gram negative bacteria cell division via an interaction between TolQ and the divisome protein FtsN
Teleha, M. (2013) · OhioLink ETD Center (Ohio Library and Information Network)

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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