Pyoverdine-mediated iron transport in Pseudomonas aeruginosa: involvement of a high-molecular-mass outer membrane protein

FEMS Microbiol Lett. 1991 Feb;62(1):1-5.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / metabolism*
  • Biological Transport, Active
  • Electrophoresis, Polyacrylamide Gel
  • Iron / metabolism*
  • Kinetics
  • Molecular Weight
  • Oligopeptides*
  • Pigments, Biological / isolation & purification
  • Pigments, Biological / metabolism*
  • Pseudomonas aeruginosa / growth & development
  • Pseudomonas aeruginosa / metabolism*

Substances

  • Bacterial Outer Membrane Proteins
  • Oligopeptides
  • Pigments, Biological
  • pyoverdin
  • Iron