In vivo evidence for FhuA outer membrane receptor interaction with the TonB inner membrane protein of Escherichia coli.
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.
Günter
K
K
Mikrobiologie II, Unversität Tübingen, FRG.
Braun
V
V
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D011991:Receptors, Virus; D015183:Restriction Mapping
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C050900:FhuA protein, E coli; D008565:Membrane Proteins; D011991:Receptors, Virus; C057616:tonB protein, Bacteria; C489181:tonB protein, E coli