A new mechanism for membrane iron transport in Pseudomonas aeruginosa.
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.
Département des Récepteurs et Protéines Membranaires UPR 9050 CNRS, ESBS, Bld Sébastien Brant, F-67400 Illkirch, Strasbourg, France. schalk@esbs.u-strasbg.fr
I J
IJ
Schalk
M A
MA
Abdallah
F
F
Pattus
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D017262:Siderophores / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; C082326:FpvA protein, Pseudomonas aeruginosa; D017262:Siderophores; D007501:Iron