FoxB of Pseudomonas aeruginosa functions in the utilization of the xenosiderophores ferrichrome, ferrioxamine B, and schizokinen: evidence for transport redundancy at the inner membrane.
Expression of the inner membrane protein FoxB (PA2465) of Pseudomonas aeruginosa in mutants of Sinorhizobium meliloti that are defective in the utilization of ferrichrome, ferrioxamine B, and schizokinen resulted in the restoration of siderophore utilization. Mutagenesis of foxB in P. aeruginosa did not abolish siderophore utilization, suggesting that the function is redundant.
Cuív
Páraic O
PO
School of Biotechnology, Dublin City University, Glasnevin, Dublin 9, Ireland.
Keogh
Damien
D
Clarke
Paul
P
O'Connell
Michael
M
D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D003676:Deferoxamine / Q000378:metabolism*; D005290:Ferric Compounds / Q000378:metabolism*; D005291:Ferrichrome / Q000378:metabolism*; D006877:Hydroxamic Acids / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D017262:Siderophores / Q000378:metabolism*
D001426:Bacterial Proteins; D005290:Ferric Compounds; D006877:Hydroxamic Acids; D017262:Siderophores; D005291:Ferrichrome; C000766:schizokinen; C002577:ferrioxamine B; D003676:Deferoxamine