Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence.
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Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriaeMetal stoichiometry and functional studies of the diphtheria toxin repressorCharacterization of the iron-regulated desA promoter of Streptomyces pilosus as a system for controlled gene expression in actinomycetesSolution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor proteinCrystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domainSolution Structure of Escherichia coli FeoA and Its Potential Role in Bacterial Ferrous Iron TransportMotion of the DNA-binding domain with respect to the core of the diphtheria toxin repressor (DtxR) revealed in the crystal structures of apo- and holo-DtxRFunctional studies of the Mycobacterium tuberculosis iron-dependent regulatorCoordinate regulation of siderophore and exotoxin A production: molecular cloning and sequencing of the Pseudomonas aeruginosa fur geneIsolation and characterization of iron-independent positive dominant mutants of the diphtheria toxin repressor DtxRConstruction and characterization of transposon insertion mutations in Corynebacterium diphtheriae that affect expression of the diphtheria toxin repressor (DtxR).SirR, a novel iron-dependent repressor in Staphylococcus epidermidisBiology and molecular epidemiology of diphtheria toxin and the tox gene.Disordered to ordered folding in the regulation of diphtheria toxin repressor activity.Genetic characterization of a Streptococcus mutans LraI family operon and role in virulence.Both Corynebacterium diphtheriae DtxR(E175K) and Mycobacterium tuberculosis IdeR(D177K) are dominant positive repressors of IdeR-regulated genes in M. tuberculosis.Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers.Genome organization and pathogenicity of Corynebacterium diphtheriae C7(-) and PW8 strains.Transcription of the contiguous sigB, dtxR, and galE genes in Corynebacterium diphtheriae: evidence for multiple transcripts and regulation by environmental factors.The src homology 3-like domain of the diphtheria toxin repressor (DtxR) modulates repressor activation through interaction with the ancillary metal ion-binding siteCharacterization of the role of the divalent metal ion-dependent transcriptional repressor MntR in the virulence of Staphylococcus aureusMolecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibacterium lactofermentum.Characterization of mutations that inactivate the diphtheria toxin repressor gene (dtxR).Determination of the minimal essential nucleotide sequence for diphtheria tox repressor binding by in vitro affinity selection.Cloning, sequence, and footprint analysis of two promoter/operators from Corynebacterium diphtheriae that are regulated by the diphtheria toxin repressor (DtxR) and iron.Effect of iron availability on expression of the Bradyrhizobium japonicum hemA geneMetalloregulation in Bacillus subtilis: isolation and characterization of two genes differentially repressed by metal ionsMobile effector proteins on phage genomes.IdeR in mycobacteria: from target recognition to physiological function.Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR.Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor.Cloning of a Corynebacterium diphtheriae iron-repressible gene that shares sequence homology with the AhpC subunit of alkyl hydroperoxide reductase of Salmonella typhimuriumCharacterization of an iron-regulated promoter involved in desferrioxamine B synthesis in Streptomyces pilosus: repressor-binding site and homology to the diphtheria toxin gene promoter.Ironing Out the Unconventional Mechanisms of Iron Acquisition and Gene Regulation in Chlamydia.Comparison of high-resolution structures of the diphtheria toxin repressor in complex with cobalt and zinc at the cation-anion binding site.
P2860
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P2860
Specific binding of the diphtheria tox regulatory element DtxR to the tox operator requires divalent heavy metal ions and a 9-base-pair interrupted palindromic sequence.
description
article científic
@ca
article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 1992
@en
vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Specific binding of the diphth ...... errupted palindromic sequence.
@en
Specific binding of the diphth ...... errupted palindromic sequence.
@nl
type
label
Specific binding of the diphth ...... errupted palindromic sequence.
@en
Specific binding of the diphth ...... errupted palindromic sequence.
@nl
prefLabel
Specific binding of the diphth ...... errupted palindromic sequence.
@en
Specific binding of the diphth ...... errupted palindromic sequence.
@nl
P2093
P2860
P356
P1476
Specific binding of the diphth ...... errupted palindromic sequence.
@en
P2093
P2860
P304
P356
10.1073/PNAS.89.13.5897
P407
P577
1992-07-01T00:00:00Z