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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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MUTANTS OF ESCHERICHIA COLI REQUIRING METHIONINE OR VITAMIN B 12
Davis, B. D., & Mingioli, E. S. (1950) · Journal of Bacteriology · doi:10.1128/jb.60.1.17-28.1950 · Cited by 2,894
Novel iron uptake system specified by ColV plasmids: an important component in the virulence of invasive strains of Escherichia coli
WILLIAMS, P. H. (1979) · Infection and Immunity · doi:10.1128/iai.26.3.925-932.1979 · Cited by 343
Different Mechanisms of Energy Coupling for the Shock-sensitive and Shock-resistant Amino Acid Permeases of Escherichia coli
Berger, E. A., & HEPPEL, L. A. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42031-0 · Cited by 340
The tol gene products and the import of macronmolecules into Escherichia coli
Webster, R. E. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb01873.x · Cited by 259
TonB and the Gram‐negative dilemma
Postle, K. (1990) · Molecular Microbiology · doi:10.1111/j.1365-2958.1990.tb00561.x · Cited by 213
Membrane receptor dependent iron transport in Escherichia coli
Hantke, K., & Braun, V. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80771-x · Cited by 191
Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB
Fischer, E., Günter, K., & Braun, V. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.9.5127-5134.1989 · Cited by 180
Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli
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Formation of a Gated Channel by a Ligand-Specific Transport Protein in the Bacterial Outer Membrane
Rutz, J. M., Liu, J., Lyons, J. A., Goranson, J., Armstrong, S. K., McIntosh, M. A., Feix, J. B., & Klebba, P. E. (1992) · Science · doi:10.1126/science.1411544 · Cited by 165
Transport of vitamin B12 in Escherichia coli. Some observations on the roles of the gene products of BtuC and TonB.
Reynolds, P. R., Mottur, G. P., & Bradbeer, C. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85667-3 · Cited by 141
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Analysis of Haptoglobin and Hemoglobin-Haptoglobin Interactions with the Neisseria meningitidis TonB-Dependent Receptor HpuAB by Flow Cytometry
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Dimerization of TonB Is Not Essential for Its Binding to the Outer Membrane Siderophore Receptor FhuA of Escherichia coli
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In Vivo Synthesis of the Periplasmic Domain of TonB Inhibits Transport through the FecA and FhuA Iron Siderophore Transporters of Escherichia coli
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Electrochemical communication in biofilm of bacterial community
Manna, S., Ghanty, C., Baindara, P., Barik, T. K., & Mandal, S. M. (2020) · Journal of Basic Microbiology · doi:10.1002/jobm.202000340 · Cited by 45
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Wiggerich, H.-G., Klauke, B., Köplin, R., Priefer, U. B., & Pühler, A. (1997) · Journal of Bacteriology · doi:10.1128/jb.179.22.7103-7110.1997 · Cited by 43
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Wiggerich, H.-G., & Pühler, A. (2000) · Microbiology · doi:10.1099/00221287-146-5-1053 · Cited by 42
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Rhodes, E. R., Menke, S. M., Shoemaker, C. J., Tomaras, A. P., McGillivary, G., & Actis, L. A. (2007) · BioMetals · doi:10.1007/s10534-006-9058-3 · Cited by 40
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Pilsl, H., & Braun, V. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.23.6966-6972.1995 · Cited by 40
Spectroscopic Observations of Ferric Enterobactin Transport
Cao, Z., Warfel, P., Newton, S. M. C., & Klebba, P. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210360200 · Cited by 39
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Active transport by customized beta-barrels.
Postle, K. (1999) · Nature Structural Biology · doi:10.1038/4869 · Cited by 39
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TonB of Escherichia coli activates FhuA through interaction with the β-barrel a aThe GenBank accession number for the sequence reported in this paper is Y15319.
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Interactions of haemoglobin with the Neisseria meningitidis receptor HpuAB: the role of TonB and an intact proton motive force
Rohde, K. H., Gillaspy, A. F., Hatfield, M. D., Lewis, L. A., & Dyer, D. W. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02745.x · Cited by 37

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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