Characterization of the stability functions and inverted repeat structure X3 of the IncFI plasmid ColV2-K94

1986 ◽  
Vol 32 (10) ◽  
pp. 806-813
Author(s):  
Peter C. Weber ◽  
Sunil Palchaudhuri
Keyword(s):  
Outer Membrane ◽  
Inverted Repeat ◽  
Iron Uptake ◽  
Membrane Receptor ◽  
Outer Membrane Receptor ◽  
Plasmid Maintenance ◽  
Stability Functions ◽  
Repeat Structure ◽  
The Stability

A region of the IncFI plasmid ColV2-K94 which showed homology to the sop partitioning genes of F was cloned and characterized in an attempt to study the stability functions of this element. The sop region contained the incD incompatibility determinant common to many IncFI plasmids, but could not confer on ColV2-K94 miniplasmids the same stable inheritance found in the intact ColV2-K94; thus, other functions appear to be required for efficient plasmid maintenance. Adjacent to the area of sop homology was the X3 region, which was found to contain three inverted IS1-like sequences. The X3 region of ColV2-K94 was similar in organization to the aerobactin iron uptake region of ColV3-K30, but ColV2-K94 lacked the ability to synthesize either the aerobactin siderophore or its outer membrane receptor.

A new mechanism for membrane iron transport in Pseudomonas aeruginosa

2002 ◽  
Vol 30 (4) ◽  
pp. 702-705 ◽  
Author(s):  
I.J. Schalk ◽  
M. A. Abdallah ◽  
F. Pattus
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Iron Uptake ◽  
Iron Transport ◽  
Membrane Receptor ◽  
Gram Negative Bacteria ◽  
Outer Membrane Receptor ◽  
Uptake Mechanism ◽  
Atp Binding Cassette Transporter ◽  
Biophysical Studies

Various biochemical and biophysical studies have demonstrated the existence of a novel iron-uptake mechanism in Pseudomonas aeruginosa, different from that generally described for ferrichrome and ferric-enterobactin in Escherichia coli. This new iron-uptake mechanism involves all the proteins generally reported to be involved in the uptake of ferric-siderophore complexes in Gram-negative bacteria (i.e. the outer membrane receptor, periplasmic binding protein and ATP-binding-cassette transporter), but differs in the behaviour of the siderophore. One of the key features of this process is the binding of iron-free pyoverdin to the outer membrane receptor FpvA in conditions of iron deficiency.

scholarly journals Characterization of a Gene Encoding the Outer Membrane Receptor for Ferric Enterobactin in Aeromonas hydrophila ATCC 7966T

2013 ◽  
Vol 77 (2) ◽  
pp. 353-360 ◽  
Author(s):  
Tatsuya FUNAHASHI ◽  
Tomotaka TANABE ◽  
Katsushiro MIYAMOTO ◽  
Hiroshi TSUJIBO ◽  
Jun MAKI ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Aeromonas Hydrophila ◽  
Membrane Receptor ◽  
Outer Membrane Receptor ◽  
Gene Encoding

scholarly journals Identification and characterization of an iron-regulated gene, chtA, required for the utilization of the xenosiderophores aerobactin, rhizobactin 1021 and schizokinen by Pseudomonas aeruginosa

Microbiology ◽  
2006 ◽  
Vol 152 (4) ◽  
pp. 945-954 ◽  
Author(s):  
Páraic Ó Cuív ◽  
Paul Clarke ◽  
Michael O'Connell
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Outer Membrane ◽  
Membrane Receptor ◽  
Outer Membrane Receptor ◽  
Significant Similarity ◽  
Hydroxamate Siderophores ◽  
Insertional Inactivation ◽  
Titration Assay

Pseudomonas aeruginosa utilizes several xenosiderophores under conditions of iron limitation, including the citrate hydroxamate siderophore aerobactin. Analysis of the P. aeruginosa genome sequence revealed the presence of two genes, chtA (PA4675) and PA1365, encoding proteins displaying significant similarity to the aerobactin outer-membrane receptor, IutA, of Escherichia coli. The chtA and PA1365 genes were mutated by insertional inactivation and it was demonstrated that ChtA is the outer-membrane receptor for aerobactin. ChtA also mediated the utilization of rhizobactin 1021 and schizokinen, which are structurally similar to aerobactin. In contrast to the utilization of other xenosiderophores by P. aeruginosa, there was no apparent redundancy in the utilization of aerobactin, rhizobactin 1021 and schizokinen. The utilization of citrate hydroxamate siderophores by P. aeruginosa was demonstrated to be TonB1 dependent. A Fur box was identified in the region directly upstream of chtA and it was demonstrated by the in vivo Fur titration assay that this region is capable of binding Fur and accordingly that expression of chtA is iron regulated. The PA1365 mutant was unaffected in the utilization of citrate hydroxamate siderophores.

scholarly journals Pumping iron: mechanisms for iron uptake by Campylobacter

Microbiology ◽  
2009 ◽  
Vol 155 (10) ◽  
pp. 3157-3165 ◽  
Author(s):  
Claire E. Miller ◽  
Peter H. Williams ◽  
Julian M. Ketley
Keyword(s):  
Outer Membrane ◽  
Molecular Characterization ◽  
Iron Uptake ◽  
Receptor Protein ◽  
Outer Membrane Receptor ◽  
Inner Membrane ◽  
Putative Receptor ◽  
Successful Colonization ◽  
Insight Into

Campylobacter requires iron for successful colonization of the host. In the last 7 years, a wealth of data has been generated allowing detailed molecular characterization of Campylobacter iron-uptake systems. Several exogenous siderophores have been identified as sources of ferric iron for Campylobacter. Ferri-enterochelin uptake requires both the outer-membrane receptor protein CfrA and the inner-membrane ABC transporter system CeuBCDE. Ferrichrome has been shown to support growth of some Campylobacter jejuni strains and the presence of homologues of Escherichia coli fhuABD genes was proposed; the Cj1658–Cj1663 system appears to be involved in the uptake of ferri-rhodotorulic acid. In addition to siderophores, the importance of host iron sources was highlighted by recent studies demonstrating that C. jejuni can exploit haem compounds and the transferrins using ChuABCDZ and Cj0173c–Cj0178, respectively. An additional putative receptor, Cj0444, present in some, but not all, strains has not yet been characterized. Following diffusion through the outer membrane, inner-membrane transport of ferrous iron can occur via the FeoB protein. While it may be assumed that all systems are not essential, there is growing evidence supporting the need for multiple iron-uptake systems for successful host colonization by Campylobacter. In light of this, comparative molecular characterization of iron systems in all Campylobacter strains is necessary to gain further insight into the pathogenesis of members of this genus.

Characterization of the cloacin DF13/aerobactin outer membrane receptor protein of Escherichia coli (pFS8)

1985 ◽  
Vol 51 (5-6) ◽  
pp. 553-554
Author(s):  
Willy J. A. Krone ◽  
Freek Stegehuis ◽  
Frits K. de Graaf ◽  
Bauke Oudega
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Receptor ◽  
Receptor Protein ◽  
Outer Membrane Receptor
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