Demonstration of an iron-siderophore-binding protein in the outer membrane of Pseudomonas aeruginosa.
Outer membranes prepared from Pseudomonas aeruginosa grown in low-iron medium bind three times as much [59Fe]pyochelin as do membranes from cells grown in high-iron medium. The deletion of pyochelin reduced 59Fe binding to background levels. Autoradiographic analysis of sodium dodecyl sulfate polyacrylamide gel electrophoretograms of outer membrane preparations previously incubated with [59Fe]pyochelin revealed that the iron-siderophore complex bound to a low-molecular-weight protein of approximately 14,000.
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D008970:Molecular Weight; D010636:Phenols / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000032:analysis*; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013844:Thiazoles
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D008565:Membrane Proteins; D010636:Phenols; D011956:Receptors, Cell Surface; D013844:Thiazoles; C035902:siderophore receptors; C025316:pyochelin