In vivo evidence for FhuA outer membrane receptor interaction with the TonB inner membrane protein of Escherichia coli

FEBS Lett. 1990 Nov 12;274(1-2):85-8. doi: 10.1016/0014-5793(90)81335-l.


FhuA outer membrane receptor activity of Escherichia coli K-12 depends on the TonB inner membrane protein. The naturally occurring degradation of the TonB protein could be prevented by the FhuA receptor protein. Mutated TonB proteins could only be stabilized by mutated FhuA proteins when they functionally interacted in the uptake of ferrichrome across the outer membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Biological Transport
  • Cell Membrane / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Genes, Bacterial
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutagenesis, Site-Directed
  • Plasmids
  • Receptors, Virus*
  • Restriction Mapping


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Escherichia coli Proteins
  • FhuA protein, E coli
  • Membrane Proteins
  • Receptors, Virus
  • tonB protein, Bacteria
  • tonB protein, E coli