Transcriptional control of the iron-responsive fxbA gene by the mycobacterial regulator IdeR

Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis, and the iron-regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin biosynthetic pathway (E. H. Fiss, Y. Yu, and W. R. Jacobs, Jr., Mol. Microbiol. 14:557-569, 1994). We investigate...

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Published inJournal of bacteriology Vol. 181; no. 11; pp. 3402 - 3408
Main Authors Dussurget, O, Timm, J, Gomez, M, Gold, B, Yu, S, Sabol, S Z, Holmes, R K, Jacobs, Jr, W R, Smith, I
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 01.06.1999
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Abstract Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis, and the iron-regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin biosynthetic pathway (E. H. Fiss, Y. Yu, and W. R. Jacobs, Jr., Mol. Microbiol. 14:557-569, 1994). We investigated the regulation of fxbA by the mycobacterial IdeR, a homolog of the Corynebacterium diphtheriae iron regulator DtxR (M. P. Schmitt, M. Predich, L. Doukhan, I. Smith, and R. K. Holmes, Infect. Immun. 63:4284-4289, 1995). Gel mobility shift experiments showed that IdeR binds to the fxbA regulatory region in the presence of divalent metals. DNase I footprinting assays indicated that IdeR binding protects a 28-bp region containing a palindromic sequence of the fxbA promoter that was identified in primer extension assays. fxbA regulation was measured in M. smegmatis wild-type and ideR mutant strains containing fxbA promoter-lacZ fusions. These experiments confirmed that fxbA expression is negatively regulated by iron and showed that inactivation of ideR results in iron-independent expression of fxbA. However, the levels of its expression in the ideR mutant were approximately 50% lower than those in the wild-type strain under iron limitation, indicating an undefined positive role of IdeR in the regulation of fxbA.
AbstractList Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis, and the iron- regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin biosynthetic pathway (E. H. Fiss, Y. Yu, and W. R. Jacobs, Jr., Mol. Microbiol. 14:557-569 1994). We investigated the regulation of fxbA by the mycobacterial IdeR, a homolog of the Corynebacterium diphtheriae iron regulator DtxR (M. P. Schmitt, M. Predich L. Doukhan, I. Smith, and R. K. Holmes, Infect. Immun. 63:4284-4289, 1995). Gel mobility shift experiments showed that IdeR binds to the fxbA regulatory region in the presence of divalent metals. DNase I footprinting assays indicated that IdeR binding protects a 28-bp region containing a palindromic sequence of the fxbA promoter that was identified in primer extension assays. fxbA regulation was measured in M. smegmatis wild-type and ideR mutant strains containing fxbA promoter-lacZ fusions. These experiments confirmed that fxbA expression is negatively regulated by iron and showed that inactivation of ideR results in iron-independent expression of fxbA. However the levels of its expression in the ideR mutant were approximately 50% lower than those in the wild- type strain under iron limitation, indicating an undefined positive role of IdeR in the regulation of fxbA.
Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis , and the iron-regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin biosynthetic pathway (E. H. Fiss, Y. Yu, and W. R. Jacobs, Jr., Mol. Microbiol. 14:557–569, 1994). We investigated the regulation of fxbA by the mycobacterial IdeR, a homolog of the Corynebacterium diphtheriae iron regulator DtxR (M. P. Schmitt, M. Predich, L. Doukhan, I. Smith, and R. K. Holmes, Infect. Immun. 63:4284–4289, 1995). Gel mobility shift experiments showed that IdeR binds to the fxbA regulatory region in the presence of divalent metals. DNase I footprinting assays indicated that IdeR binding protects a 28-bp region containing a palindromic sequence of the fxbA promoter that was identified in primer extension assays. fxbA regulation was measured in M. smegmatis wild-type and ideR mutant strains containing fxbA promoter- lacZ fusions. These experiments confirmed that fxbA expression is negatively regulated by iron and showed that inactivation of ideR results in iron-independent expression of fxbA . However, the levels of its expression in the ideR mutant were approximately 50% lower than those in the wild-type strain under iron limitation, indicating an undefined positive role of IdeR in the regulation of fxbA .
Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis, and the iron-regulated fxbA gene encodes a putative formyltransferase, an essential enzyme in the exochelin biosynthetic pathway.
Author Gomez, M
Sabol, S Z
Holmes, R K
Jacobs, Jr, W R
Dussurget, O
Gold, B
Smith, I
Timm, J
Yu, S
AuthorAffiliation TB Center, Public Health Research Institute, 1 and Department of Microbiology, New York University Medical Center, 3 New York, New York 10016; UFR de Biochimie, Université Paris 7, 75251 Paris Cedex 05, France 2 ; Department of Microbiology and Immunology, Howard Hughes Medical Institute, Albert Einstein College of Medicine, Bronx, New York 10461 4 ; Section of Gene Structure and Regulation, Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892 5 ; and Department of Microbiology, University of Colorado Health Sciences Center, Denver, Colorado 80262 6
AuthorAffiliation_xml – name: TB Center, Public Health Research Institute, 1 and Department of Microbiology, New York University Medical Center, 3 New York, New York 10016; UFR de Biochimie, Université Paris 7, 75251 Paris Cedex 05, France 2 ; Department of Microbiology and Immunology, Howard Hughes Medical Institute, Albert Einstein College of Medicine, Bronx, New York 10461 4 ; Section of Gene Structure and Regulation, Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892 5 ; and Department of Microbiology, University of Colorado Health Sciences Center, Denver, Colorado 80262 6
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/10348851$$D View this record in MEDLINE/PubMed
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Corresponding author. Mailing address: TB Center, Public Health Research Institute, 455 First Ave., New York, NY 10016. Phone: (212) 578-0867. Fax: (212) 578-0804. E-mail: smitty@phri.nyu.edu.
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Snippet Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis, and the iron-regulated fxbA gene encodes a putative formyltransferase, an...
Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis , and the iron-regulated fxbA gene encodes a putative formyltransferase, an...
Exochelin is the primary extracellular siderophore of Mycobacterium smegmatis, and the iron- regulated fxbA gene encodes a putative formyltransferase, an...
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Index Database
StartPage 3402
SubjectTerms Bacteria
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriology
Base Sequence
beta-Galactosidase - genetics
beta-Galactosidase - metabolism
Binding Sites
Cations, Divalent - pharmacology
Cells
Corynebacterium diphtheriae
DNA Footprinting
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Enzymes
Gene Expression Regulation, Bacterial - drug effects
Genes
Genes, Bacterial - genetics
Genes, Reporter
Genetics and Molecular Biology
Hydroxymethyl and Formyl Transferases - genetics
Iron - pharmacology
Mutation
Mycobacterium - drug effects
Mycobacterium - enzymology
Mycobacterium - genetics
Mycobacterium smegmatis
Promoter Regions, Genetic - genetics
Protein Binding - drug effects
Repressor Proteins
Response Elements - genetics
RNA, Messenger - analysis
RNA, Messenger - genetics
Sequence Homology, Amino Acid
Transcription, Genetic - drug effects
Transcription, Genetic - genetics
Title Transcriptional control of the iron-responsive fxbA gene by the mycobacterial regulator IdeR
URI https://www.ncbi.nlm.nih.gov/pubmed/10348851
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https://pubmed.ncbi.nlm.nih.gov/PMC93806
Volume 181
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