Identification of the Periplasmic Cobalamin-Binding Protein BtuF of Escherichia coli

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Published inJournal of Bacteriology Vol. 184; no. 3; pp. 706 - 717
Main Authors Cadieux, Nathalie, Bradbeer, Clive, Reeger-Schneider, Eva, Köster, Wolfgang, Mohanty, Arun K, Wiener, Michael C, Kadner, Robert J
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.02.2002
Subjects
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
ATP-Binding Cassette Transporters
Bacteria
Bacterial Proteins
Bacteriology
Biological Transport
btuC gene
btuD gene
btuF gene
BtuF protein
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Division
Cloning, Molecular
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Methyltransferases
Mutation
N-Glycosyl Hydrolases - genetics
Periplasm - metabolism
Periplasmic Binding Proteins
Phenotype
Physiology and Metabolism
Proteins
Recombinant Proteins - metabolism
Suppression, Genetic
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 Cells of Escherichia coli take up vitamin B12 (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of CN-Cbl across the outer membrane and its accumulation in the periplasm is mediated by the TonB-dependent transporter BtuB.
Cells of Escherichia coli take up vitamin B(12) (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of CN-Cbl across the outer membrane and its accumulation in the periplasm is mediated by the TonB-dependent transporter BtuB. Transport across the cytoplasmic membrane (CM) requires the BtuC and BtuD proteins, which are most related in sequence to the transmembrane and ATP-binding cassette proteins of periplasmic permeases for iron-siderophore transport. Unlike the genetic organization of most periplasmic permeases, a candidate gene for a periplasmic Cbl-binding protein is not linked to the btuCED operon. The open reading frame termed yadT in the E. coli genomic sequence is related in sequence to the periplasmic binding proteins for iron-siderophore complexes and was previously implicated in CN-Cbl uptake in Salmonella. The E. coli yadT product, renamed BtuF, is shown here to participate in CN-Cbl uptake. BtuF protein, expressed with a C-terminal His(6) tag, was shown to be translocated to the periplasm concomitant with removal of a signal sequence. CN-Cbl-binding assays using radiolabeled substrate or isothermal titration calorimetry showed that purified BtuF binds CN-Cbl with a binding constant of around 15 nM. A null mutation in btuF, but not in the flanking genes pfs and yadS, strongly decreased CN-Cbl utilization and transport into the cytoplasm. The growth response to CN-Cbl of the btuF mutant was much stronger than the slight impairment previously described for btuC, btuD, or btuF mutants. Hence, null mutations in btuC and btuD were constructed and revealed that the btuC mutant had a strong impairment similar to that of the btuF mutant, whereas the btuD defect was less pronounced. All mutants with defective transport across the CM gave rise to frequent suppressor variants which were able to respond at lower levels of CN-Cbl but were still defective in transport across the CM. These results finally establish the identity of the periplasmic binding protein for Cbl uptake, which is one of few cases where the components of a periplasmic permease are genetically separated.
Cells of Escherichia coli take up vitamin B 12 (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of CN-Cbl across the outer membrane and its accumulation in the periplasm is mediated by the TonB-dependent transporter BtuB. Transport across the cytoplasmic membrane (CM) requires the BtuC and BtuD proteins, which are most related in sequence to the transmembrane and ATP-binding cassette proteins of periplasmic permeases for iron-siderophore transport. Unlike the genetic organization of most periplasmic permeases, a candidate gene for a periplasmic Cbl-binding protein is not linked to the btuCED operon. The open reading frame termed yadT in the E. coli genomic sequence is related in sequence to the periplasmic binding proteins for iron-siderophore complexes and was previously implicated in CN-Cbl uptake in Salmonella . The E. coli yadT product, renamed BtuF, is shown here to participate in CN-Cbl uptake. BtuF protein, expressed with a C-terminal His 6 tag, was shown to be translocated to the periplasm concomitant with removal of a signal sequence. CN-Cbl-binding assays using radiolabeled substrate or isothermal titration calorimetry showed that purified BtuF binds CN-Cbl with a binding constant of around 15 nM. A null mutation in btuF , but not in the flanking genes pfs and yadS , strongly decreased CN-Cbl utilization and transport into the cytoplasm. The growth response to CN-Cbl of the btuF mutant was much stronger than the slight impairment previously described for btuC , btuD , or btuF mutants. Hence, null mutations in btuC and btuD were constructed and revealed that the btuC mutant had a strong impairment similar to that of the btuF mutant, whereas the btuD defect was less pronounced. All mutants with defective transport across the CM gave rise to frequent suppressor variants which were able to respond at lower levels of CN-Cbl but were still defective in transport across the CM. These results finally establish the identity of the periplasmic binding protein for Cbl uptake, which is one of few cases where the components of a periplasmic permease are genetically separated.
Cells of Escherichia coli take up vitamin B sub(12) (cyano-cobalamin [CN- Cbl]) and iron chelates by use of sequential active transport processes. Transport of CN-Cbl across the outer membrane and its accumulation in the periplasm is mediated by the TonB-dependent transporter BtuB. Transport across the cytoplasmic membrane (CM) requires the BtuC and BtuD proteins, which are most related in sequence to the transmembrane and ATP-binding cassette proteins of periplasmic permeases for iron-siderophore transport. Unlike the genetic organization of most periplasmic permeases, a candidate gene for a periplasmic Cbl-binding protein is not linked to the btuCED operon. The open reading frame termed yadT in the E. coli genomic sequence is related in sequence to the periplasmic binding proteins for iron-siderophore complexes and was previously implicated in CN-Cbl uptake in Salmonella. The E. coli yadT product, renamed BtuF, is shown here to participate in CN-Cbl uptake. BtuF protein, expressed with a C-terminal His sub(6) tag, was shown to be translocated to the periplasm concomitant with removal of a signal sequence. CN-Cbl-binding assays using radiolabeled substrate or isothermal titration calorimetry showed that purified BtuF binds CN-Cbl with a binding constant of around 15 nM. A null mutation in btuF, but not in the flanking genes pfs and yadS, strongly decreased CN-Cbl utilization and transport into the cytoplasm. The growth response to CN-Cbl of the btuF mutant was much stronger than the slight impairment previously described for btuC, btuD, or btuF mutants. Hence, null mutations in btuC and btuD were constructed and revealed that the btuC mutant had a strong impairment similar to that of the btuF mutant, whereas the btuD defect was less pronounced. All mutants with defective transport across the CM gave rise to frequent suppressor variants which were able to respond at lower levels of CN-Cbl but were still defective in transport across the CM. These results finally establish the identity of the periplasmic binding protein for Cbl uptake, which is one of few cases where the components of a periplasmic permease are genetically separated.
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       
ABSTRACT Cells of Escherichia coli take up vitamin B 12 (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of CN-Cbl across the outer membrane and its accumulation in the periplasm is mediated by the TonB-dependent transporter BtuB. Transport across the cytoplasmic membrane (CM) requires the BtuC and BtuD proteins, which are most related in sequence to the transmembrane and ATP-binding cassette proteins of periplasmic permeases for iron-siderophore transport. Unlike the genetic organization of most periplasmic permeases, a candidate gene for a periplasmic Cbl-binding protein is not linked to the btuCED operon. The open reading frame termed yadT in the E. coli genomic sequence is related in sequence to the periplasmic binding proteins for iron-siderophore complexes and was previously implicated in CN-Cbl uptake in Salmonella . The E. coli yadT product, renamed BtuF, is shown here to participate in CN-Cbl uptake. BtuF protein, expressed with a C-terminal His 6 tag, was shown to be translocated to the periplasm concomitant with removal of a signal sequence. CN-Cbl-binding assays using radiolabeled substrate or isothermal titration calorimetry showed that purified BtuF binds CN-Cbl with a binding constant of around 15 nM. A null mutation in btuF , but not in the flanking genes pfs and yadS , strongly decreased CN-Cbl utilization and transport into the cytoplasm. The growth response to CN-Cbl of the btuF mutant was much stronger than the slight impairment previously described for btuC , btuD , or btuF mutants. Hence, null mutations in btuC and btuD were constructed and revealed that the btuC mutant had a strong impairment similar to that of the btuF mutant, whereas the btuD defect was less pronounced. All mutants with defective transport across the CM gave rise to frequent suppressor variants which were able to respond at lower levels of CN-Cbl but were still defective in transport across the CM. These results finally establish the identity of the periplasmic binding protein for Cbl uptake, which is one of few cases where the components of a periplasmic permease are genetically separated.
Author Wolfgang Köster
Eva Reeger-Schneider
Nathalie Cadieux
Arun K. Mohanty
Michael C. Wiener
Robert J. Kadner
Clive Bradbeer
AuthorAffiliation Department of Microbiology, 1 Department of Biochemistry and Molecular Genetics, 2 Department of Molecular Physiology and Biological Physics, School of Medicine, University of Virginia, Charlottesville, Virginia 22908-0734, 4 Mikrobiologie/Membranphysiologie, Universität Tübingen, D-72076 Tübingen, Germany 3
AuthorAffiliation_xml – name: Department of Microbiology, 1 Department of Biochemistry and Molecular Genetics, 2 Department of Molecular Physiology and Biological Physics, School of Medicine, University of Virginia, Charlottesville, Virginia 22908-0734, 4 Mikrobiologie/Membranphysiologie, Universität Tübingen, D-72076 Tübingen, Germany 3
Author_xml – sequence: 1
  givenname: Nathalie
  surname: Cadieux
  fullname: Cadieux, Nathalie
  organization: Department of Microbiology, School of Medicine, University of Virginia, Charlottesville, Virginia 22908-0734, USA
– sequence: 2
  givenname: Clive
  surname: Bradbeer
  fullname: Bradbeer, Clive
– sequence: 3
  givenname: Eva
  surname: Reeger-Schneider
  fullname: Reeger-Schneider, Eva
– sequence: 4
  givenname: Wolfgang
  surname: Köster
  fullname: Köster, Wolfgang
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  surname: Mohanty
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  fullname: Wiener, Michael C
– sequence: 7
  givenname: Robert J
  surname: Kadner
  fullname: Kadner, Robert J
BackLink https://www.ncbi.nlm.nih.gov/pubmed/11790740$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: Department of Microbiology, University of Virginia School of Medicine, P.O. Box 800734, Charlottesville, VA 22908-0734. Phone: (434) 924-2532. Fax: (434) 982-1071. E-mail: rjk@virginia.edu.
Present address: Uhrbacherstrasse 16, D-70374 Stuttgart, Germany.
Present address: Environmental Microbiology and Molecular Ecotoxicology, Swiss Federal Institute for Environmental Science and Technology, CH-8600 Dübendorf, Switzerland.
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PublicationTitle Journal of Bacteriology
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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...
Cells of Escherichia coli take up vitamin B(12) (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of...
ABSTRACT Cells of Escherichia coli take up vitamin B 12 (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport...
Cells of Escherichia coli take up vitamin B12 (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of CN-Cbl...
Cells of Escherichia coli take up vitamin B sub(12) (cyano-cobalamin [CN- Cbl]) and iron chelates by use of sequential active transport processes. Transport of...
Cells of Escherichia coli take up vitamin B 12 (cyano-cobalamin [CN-Cbl]) and iron chelates by use of sequential active transport processes. Transport of...
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SubjectTerms 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
ATP-Binding Cassette Transporters
Bacteria
Bacterial Proteins
Bacteriology
Biological Transport
btuC gene
btuD gene
btuF gene
BtuF protein
Carrier Proteins - genetics
Carrier Proteins - metabolism
Cell Division
Cloning, Molecular
Escherichia coli
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins
Methyltransferases
Mutation
N-Glycosyl Hydrolases - genetics
Periplasm - metabolism
Periplasmic Binding Proteins
Phenotype
Physiology and Metabolism
Proteins
Recombinant Proteins - metabolism
Suppression, Genetic
vitamin B
Vitamin B 12 - metabolism
Title Identification of the Periplasmic Cobalamin-Binding Protein BtuF of Escherichia coli
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