Residues involved in FecR binding are localized on one side of the FecA signaling domain in Escherichia coli.
Ferric citrate transport in Escherichia coli involves proteins encoded by the fec genes, including the transport and signaling protein FecA and the signal transducing protein FecR. Randomly isolated FecA point mutants showed a reduced interaction with FecR and a reduced transcription initiation of the ferric citrate transport genes. The mutations were localized on one side of the FecA signaling domain, which might form the interface to FecR. Some of the mutants showed strongly reduced iron transport rates, which suggests that the signaling domain affects the structure of the FecA transporter domain.
Breidenstein
Elena
E
Microbiology/Membrane Physiology, University of Tübingen, D-72076 Tübingen, Germany.
Mahren
Susanne
S
Braun
Volkmar
V
D001692:Biological Transport; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005290:Ferric Compounds / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000378:metabolism*; D008958:Models, Molecular; D017354:Point Mutation; D011485:Protein Binding; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D012808:Sigma Factor / Q000378:metabolism*
D029968:Escherichia coli Proteins; C028589:FecA protein, E coli; C093541:FecR protein, E coli; D005290:Ferric Compounds; D026901:Membrane Transport Proteins; D011956:Receptors, Cell Surface; D012808:Sigma Factor; C025314:ferric citrate