Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function

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Published inJournal of Bacteriology Vol. 177; no. 17; pp. 4829 - 4835
Main Authors Kadner, R J, Heller, K J
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.09.1995
Subjects
Bacterial Outer Membrane Proteins - biosynthesis
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Bacterial Proteins - biosynthesis
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Binding, Competitive
Biochemistry
Biological Transport - drug effects
Carrier Proteins - metabolism
Chelating Agents - pharmacology
Escherichia coli
Escherichia coli - drug effects
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Ferrichrome - metabolism
Iron - metabolism
Membrane Proteins - biosynthesis
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Transport Proteins
Membranes
Proteins
Receptors, Peptide - biosynthesis
Receptors, Peptide - genetics
Receptors, Peptide - metabolism
Receptors, Virus - biosynthesis
Receptors, Virus - genetics
Receptors, Virus - metabolism
Vitamin B
Vitamin B 12 - metabolism
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Abstract Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology.   For an alternate route to JB .asm.org, visit: JB       
AbstractList Vitamin B sub(12) (CN-Cbl) and iron-siderophore complexes are transported into Escherichia coli in two energy-dependent steps. The first step is mediated by substrate-specific outer membrane transport proteins and the energy-coupling TonB protein complex, and the second step uses separate periplasmic permeases for transport across the cytoplasmic membrane. Genetic and biochemical evidence suggests that the TonB-dependent outer membrane transporters contact TonB directly, and thus they might compete for limiting amounts of functional TonB. The transport of iron-siderophore complexes, such as ferrichrome, causes a partial decrease in the rate of CN-Cbl transport. Although CN-Cbl uptake does not inhibit ferrichrome uptake in wild-type cells, in which the amount of the outer membrane ferrichrome transporter FhuA far exceeds that of the cobalamin transporter BtuB, CN-Cbl does inhibit ferrichrome uptake when BtuB is overexpressed from a multicopy plasmid. This inhibition by CN-Cbl is increased when the expression of FhuA and TonB is repressed by growth with excess iron and is eliminated when BtuB synthesis is repressed by CN-Cbl. The mutual inhibition of CN-Cbl and ferrichrome uptake is overcome by increased expression of TonB. Additional evidence for interaction of the Cbl and iron transport systems is provided by the strong stimulation of the BtuB- and TonB-dependent transport of CN-Cbl into a nonexchangeable, presumably cytoplasmic pool by preincubation of cells with the iron(II) chelator 2,2'-dipyridyl. Other metal ion chelators inhibited CN-Cbl uptake across the outer membrane. Although the effects of chelators are multiple and complex, they indicate competition or interaction among TonB-dependent transport systems.
Vitamin B12 (CN-Cbl) and iron-siderophore complexes are transported into Escherichia coli in two energy-dependent steps. The first step is mediated by substrate-specific outer membrane transport proteins and the energy-coupling TonB protein complex, and the second step uses separate periplasmic permeases for transport across the cytoplasmic membrane. Genetic and biochemical evidence suggests that the TonB-dependent outer membrane transporters contact TonB directly, and thus they might compete for limiting amounts of functional TonB. The transport of iron-siderophore complexes, such as ferrichrome, causes a partial decrease in the rate of CN-Cbl transport. Although CN-Cbl uptake does not inhibit ferrichrome uptake in wild-type cells, in which the amount of the outer membrane ferrichrome transporter FhuA far exceeds that of the cobalamin transporter BtuB, CN-Cbl does inhibit ferrichrome uptake when BtuB is overexpressed from a multicopy plasmid. This inhibition by CN-Cbl is increased when the expression of FhuA and TonB is repressed by growth with excess iron and is eliminated when BtuB synthesis is repressed by CN-Cbl. The mutual inhibition of CN-Cbl and ferrichrome uptake is overcome by increased expression of TonB. Additional evidence for interaction of the Cbl and iron transport systems is provided by the strong stimulation of the BtuB- and TonB-dependent transport of CN-Cbl into a nonexchangeable, presumably cytoplasmic pool by preincubation of cells with the iron(II) chelator 2,2'-dipyridyl. Other metal ion chelators inhibited CN-Cbl uptake across the outer membrane. Although the effects of chelators are multiple and complex, they indicate competition or interaction among TonB-dependent transport systems.
Vitamin B12 and iron-siderophore complexes are transported into Escherichia coli in two energy-dependent steps. The effects of chelators indicate competition or interacton among TonB-dependent transport systems.
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Author K J Heller
R J Kadner
AuthorAffiliation Department of Microbiology, University of Virginia School of Medicine, Charlottesville 22908, USA
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SSID ssj0014452
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Snippet Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley...
Vitamin B12 (CN-Cbl) and iron-siderophore complexes are transported into Escherichia coli in two energy-dependent steps. The first step is mediated by...
Vitamin B12 and iron-siderophore complexes are transported into Escherichia coli in two energy-dependent steps. The effects of chelators indicate competition...
Vitamin B sub(12) (CN-Cbl) and iron-siderophore complexes are transported into Escherichia coli in two energy-dependent steps. The first step is mediated by...
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StartPage 4829
SubjectTerms Bacterial Outer Membrane Proteins - biosynthesis
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Bacterial Proteins - biosynthesis
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Binding, Competitive
Biochemistry
Biological Transport - drug effects
Carrier Proteins - metabolism
Chelating Agents - pharmacology
Escherichia coli
Escherichia coli - drug effects
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Ferrichrome - metabolism
Iron - metabolism
Membrane Proteins - biosynthesis
Membrane Proteins - genetics
Membrane Proteins - metabolism
Membrane Transport Proteins
Membranes
Proteins
Receptors, Peptide - biosynthesis
Receptors, Peptide - genetics
Receptors, Peptide - metabolism
Receptors, Virus - biosynthesis
Receptors, Virus - genetics
Receptors, Virus - metabolism
Vitamin B
Vitamin B 12 - metabolism
Title Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function
URI http://jb.asm.org/content/177/17/4829.abstract
https://www.ncbi.nlm.nih.gov/pubmed/7665457
https://www.proquest.com/docview/227037909
https://search.proquest.com/docview/16881186
https://search.proquest.com/docview/77492338
https://pubmed.ncbi.nlm.nih.gov/PMC177254
Volume 177
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