Sequence of Ligand Binding and Structure Change in the Diphtheria Toxin Repressor upon Activation by Divalent Transition Metals†

Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5672-5682 ◽  
Author(s):  
Vijayaraghavan Rangachari ◽  
Vedrana Marin ◽  
Ewa A. Bienkiewicz ◽  
Maria Semavina ◽  
Luis Guerrero ◽  
...  
Keyword(s):  
Transition Metals ◽  
Ligand Binding ◽  
Diphtheria Toxin ◽  
Structure Change ◽  
Diphtheria Toxin Repressor

Oxidatively Induced Reactivity of [Fe2(CO)4(κ2-dppe)(μ-pdt)]: an Electrochemical and Theoretical Study of the Structure Change and Ligand Binding Processes

2011 ◽  
Vol 50 (24) ◽  
pp. 12575-12585 ◽  
Author(s):  
Dounia Chouffai ◽  
Giuseppe Zampella ◽  
Jean-François Capon ◽  
Luca De Gioia ◽  
Frédéric Gloaguen ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Theoretical Study ◽  
Structure Change

Prolylpeptide Binding by the Prokaryotic SH3-like Domain of the Diphtheria Toxin Repressor:  A Regulatory Switch†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (1) ◽  
pp. 40-51 ◽  
Author(s):  
Gregory P. Wylie ◽  
Vijayaraghavan Rangachari ◽  
Ewa A. Bienkiewicz ◽  
Vedrana Marin ◽  
Nilakshee Bhattacharya ◽  
...  
Keyword(s):  
Diphtheria Toxin ◽  
Diphtheria Toxin Repressor

Structure of the metal-ion-activated diphtheria toxin repressor/ tox operator complex

Nature ◽  
10.1038/28893 ◽  
1998 ◽  
Vol 394 (6692) ◽  
pp. 502-506 ◽  
Author(s):  
André White ◽  
Xiaochun Ding ◽  
Johanna C. vanderSpek ◽  
John R. Murphy ◽  
Dagmar Ringe
Keyword(s):  
Diphtheria Toxin ◽  
Metal Ion ◽  
Diphtheria Toxin Repressor

scholarly journals Construction and Characterization of Transposon Insertion Mutations in Corynebacterium diphtheriae That Affect Expression of the Diphtheria Toxin Repressor (DtxR)

2002 ◽  
Vol 184 (20) ◽  
pp. 5723-5732 ◽  
Author(s):  
Diana Marra Oram ◽  
Ana Avdalovic ◽  
Randall K. Holmes
Keyword(s):  
Oxidative Stress ◽  
Diphtheria Toxin ◽  
Corynebacterium Diphtheriae ◽  
Insertion Mutant ◽  
Toxin Gene ◽  
Wild Type ◽  
Transposon Insertion ◽  
Diphtheria Toxin Repressor ◽  
Mutant Strains

ABSTRACT Transcription of the bacteriophage-borne diphtheria toxin gene tox is negatively regulated, in response to intracellular Fe2+ concentration, by the chromosomally encoded diphtheria toxin repressor (DtxR). Due to a scarcity of tools, genetic analysis of Corynebacterium diphtheriae has primarily relied on analysis of chemically induced and spontaneously occurring mutants and on the results of experiments with C. diphtheriae genes cloned in Escherichia coli or analyzed in vitro. We modified a Tn5-based mutagenesis technique for use with C. diphtheriae, and we used it to construct the first transposon insertion libraries in the chromosome of this gram-positive pathogen. We isolated two insertions that affected expression of DtxR, one 121 bp upstream of dtxR and the other within an essential region of the dtxR coding sequence, indicating for the first time that dtxR is a dispensable gene in C. diphtheriae. Both mutant strains secrete diphtheria toxin when grown in medium containing sufficient iron to repress secretion of diphtheria toxin by wild-type C. diphtheriae. The upstream insertion mutant still produces DtxR in decreased amounts and regulates siderophore secretion in response to iron in a manner similar to its wild-type parent. The mutant containing the transposon insertion within dtxR does not produce DtxR and overproduces siderophore in the presence of iron. Differences in the ability of the two mutant strains to survive oxidative stress also indicated that the upstream insertion retained slight DtxR activity, whereas the insertion within dtxR abolished DtxR activity. This is the first evidence that DtxR plays a role in protecting the cell from oxidative stress.

scholarly journals Metal stoichiometry and functional studies of the diphtheria toxin repressor

2003 ◽  
Vol 100 (7) ◽  
pp. 3808-3813 ◽  
Author(s):  
M. M. Spiering ◽  
D. Ringe ◽  
J. R. Murphy ◽  
M. A. Marletta
Keyword(s):  
Diphtheria Toxin ◽  
Functional Studies ◽  
Diphtheria Toxin Repressor
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