(Q57753173)

English

The SH3-like domain switches its interaction partners to modulate the repression activity of mycobacterial iron-dependent transcription regulator in response to metal ion fluctuations

scientific article published in Journal of Biological Chemistry

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scholarly article

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The SH3-like domain switches its interaction partners to modulate the repression activity of mycobacterial iron-dependent transcription regulator in response to metal ion fluctuations (English)

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object named as

Weizhe Hong

5

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object named as

Bo Peng

7

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author name string

Chong Liu

1

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Kai Mao

2

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Meng Zhang

3

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Zhaogang Sun

4

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Chuanyou Li

6

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Zengyi Chang

8

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language of work or name

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publication date

25 January 2008

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Journal of Biological Chemistry

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283

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4

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2439-53

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Bacterial iron homeostasis

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Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro

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An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response.

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The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages

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Mechanisms of iron regulation in mycobacteria: role in physiology and virulence

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ideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response

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Cloning and sequence analysis of the Corynebacterium diphtheriae dtxR homologue from Streptomyces lividans and S. pilosus encoding a putative iron repressor protein.

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Molecular cloning, DNA sequence analysis, and characterization of the Corynebacterium diphtheriae dtxR homolog from Brevibacterium lactofermentum

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The iron dependent regulatory protein IdeR (DtxR) of Rhodococcus equi

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Molecular cloning and DNA sequence analysis of a diphtheria tox iron-dependent regulatory element (dtxR) from Corynebacterium diphtheriae

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Functional studies of the Mycobacterium tuberculosis iron-dependent regulator

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Cysteine-102 is positioned in the metal binding activation site of the Corynebacterium diphtheriae regulatory element DtxR.

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Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis shows both metal binding sites fully occupied

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Crystal structure of a cobalt-activated diphtheria toxin repressor-DNA complex reveals a metal-binding SH3-like domain

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Crystal structure of an IdeR-DNA complex reveals a conformational change in activated IdeR for base-specific interactions

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Mechanism of metal ion activation of the diphtheria toxin repressor DtxR.

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Solution structure and peptide binding studies of the C-terminal src homology 3-like domain of the diphtheria toxin repressor protein

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Disordered to ordered folding in the regulation of diphtheria toxin repressor activity

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Transition metal ion activation of DNA binding by the diphtheria tox repressor requires the formation of stable homodimers

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Metal stoichiometry and functional studies of the diphtheria toxin repressor

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Metal-linked dimerization in the iron-dependent regulator from Mycobacterium tuberculosis

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Controlling gene expression in mycobacteria with anhydrotetracycline and Tet repressor

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Construction of a family of Mycobacterium/Escherichia coli shuttle vectors derived from pAL5000 and pACYC184: their use for cloning an antibiotic-resistance gene from Mycobacterium fortuitum.

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Oligomerization domain-directed reassembly of active dihydrofolate reductase from rationally designed fragments.

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Increasing the efficiency of SAGE adaptor ligation by directed ligation chemistry

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Predicting oligomeric assemblies: N-mers a primer.

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The closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants

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Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli

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Design and development of a novel genetic probe for the analysis of repressor-operator interactions.

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Genetic and biophysical studies of diphtheria toxin repressor (DtxR) and the hyperactive mutant DtxR(E175K) support a multistep model of activation.

1 reference

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21 January 2018

The src homology 3-like domain of the diphtheria toxin repressor (DtxR) modulates repressor activation through interaction with the ancillary metal ion-binding site

1 reference

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21 January 2018

Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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Dissecting virulence pathways of Mycobacterium tuberculosis through protein-protein association.

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Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis

1 reference

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Inter-subunit cross-linking suppressed the dynamic oligomeric dissociation of Mycobacterium tuberculosis Hsp16.3 and reduced its chaperone activity

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Stepwise disassembly and apparent nonstepwise reassembly for the oligomeric RbsD protein.

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Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis

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Disulphide bridges in globular proteins

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Identification of the primary metal ion-activation sites of the diphtheria tox repressor by X-ray crystallography and site-directed mutational analysis.

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21 January 2018

Methyl groups of thymine bases are important for nucleic acid recognition by DtxR

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Reactions of N-ethylmaleimide with peptides and amino acids

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Determination of the distance between two spin labels attached to a macromolecule

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Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways.

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Prolylpeptide binding by the prokaryotic SH3-like domain of the diphtheria toxin repressor: a regulatory switch

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A novel peptide-SH3 interaction.

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A unique set of SH3-SH3 interactions controls IB1 homodimerization

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Analysis of truncated variants of the iron dependent transcriptional regulators fromCorynebacterium diphtheriaeandMycobacterium tuberculosis

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21 January 2018

Identifiers

10.1074/JBC.M706580200

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