8-Azido-ATP labelling of the FecE protein of the<i>Escherichia coli</i>iron citrate transport system

Schultz-Hauser, Gabriele; Hove, B Van; Braun, Volkmar

doi:10.1111/j.1574-6968.1992.tb05371.x

Cited by 8 publications

(1 citation statement)

References 17 publications

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“…Among them, FecCDE and Fe 3+ dicitrate-binding periplasmic protein are related to bacterial iron transport ( 28 , 29 ), PagN is related to bacterial invasion of host cells ( 30 , 31 ), and l -idonate 5-dehydrogenase [NAD(P)(+)] is involved in l -iodic acid catabolism pathways ( 32 ), while yeeN (which encodes a conserved hypothetical protein) and yjhP (which encodes a putative methyltransferase) are most commonly found at the 3′ end of tRNA leuX islands ( 33 ). In addition, YjhP may be associated with bacterial resistance ( 34 , 35 ).…”

Section: Resultsmentioning

confidence: 99%

The DNA Phosphorothioation Restriction-Modification System Influences the Antimicrobial Resistance of Pathogenic Bacteria

Rao

Xie

et al. 2023

Microbiol Spectr

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Section: Resultsmentioning

confidence: 99%

The DNA Phosphorothioation Restriction-Modification System Influences the Antimicrobial Resistance of Pathogenic Bacteria

Rao

Xie

et al. 2023

Microbiol Spectr

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Control of Bacterial Iron Transport by Regulatory Proteins

Hantke¹,

Braun²

1998

Metal Ions in Gene Regulation

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In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence

1995

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Transport of iron (III) hydroxamates across the inner membrane of Escherichia coli depends on a binding protein-dependent transport system composed of the FhuB, C and D proteins. The FhuD protein, which is synthesized as a precursor and exported through the cytoplasmic membrane, represents the periplasmic binding protein of the system, accepting as substrates a number of hydroxamate siderophores and the antibiotic albomycin. A FhuD derivative, carrying an N-terminal His-tag sequence instead of its signal sequence and therefore not exported through the inner membrane, was purified from the cytoplasm. Functional activity, comparable to that of wild-type FhuD, was demonstrated for this His-tag-FhuD in vitro by protease protection experiments in the presence of different substrates, and in vivo by reconstitution of iron transport in a fhuD mutant strain. The experimental data demonstrate that the primary sequence of the portion corresponding to the mature FhuD contains all the information required for proper folding of the polypeptide chain into a functional solute-binding protein. Moreover, purification of modified periplasmic proteins from the cytosol may be a useful approach for recovery of many polypeptides which are normally exported across the inner membrane and can cause toxicity problems when overproduced.

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8-Azido-ATP labelling of the FecE protein of theEscherichia coliiron citrate transport system

Cited by 8 publications

References 17 publications

The DNA Phosphorothioation Restriction-Modification System Influences the Antimicrobial Resistance of Pathogenic Bacteria

The DNA Phosphorothioation Restriction-Modification System Influences the Antimicrobial Resistance of Pathogenic Bacteria

Control of Bacterial Iron Transport by Regulatory Proteins

In vivo reconstitution of an active siderophore transport system by a binding protein derivative lacking a signal sequence

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