Pyoverdine-mediated iron transport in Pseudomonas aeruginosa: involvement of a high-molecular-mass outer membrane protein.
Reduced expression of an iron-regulated outer membrane protein (IROMP) of approximate molecular mass 90,000 was observed in Pseudomonas aeruginosa concomitant with a loss of pyoverdine production in a wild type strain grown at 43 degrees C and in a mutant deficient in pyoverdine production. Consistent with an implied role in pyoverdine-mediated iron transport a mutant lacking the 90 kDa protein transported barely detectable levels of ferri-pyoverdine. Interestingly, the mutant still exhibited pyoverdine-dependent growth in an iron-deficient medium containing the synthetic iron chelator ethylene diamine-di(omicron-hydroxyphenol acetic acid) (EDDHA) suggesting that a second uptake system for ferri-pyoverdine may exist in P. aeruginosa.
Poole
K
K
Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada.
Neshat
S
S
Heinrichs
D
D
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D001693:Biological Transport, Active; D004591:Electrophoresis, Polyacrylamide Gel; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D009842:Oligopeptides; D010860:Pigments, Biological / Q000302:isolation & purification / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000254:growth & development / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D009842:Oligopeptides; D010860:Pigments, Biological; C042453:pyoverdin; D007501:Iron