Transcriptional regulation from the cell surface: conformational changes in the transmembrane protein FecR lead to altered transcription of the ferric citrate transport genes in Escherichia coli.
Ferric citrate induces the ferric citrate transport system in Escherichia coli without being taken up into cells. The cytoplasmic transmembrane protein FecR, required for the response to ferric citrate, was found to be cleaved by a cellular protease. FecR protein produced by fecR mutants impaired or constitutive in fecA transcription was protease resistant, indicating that conformational changes affect proper functioning of FecR.
Wriedt
K
K
Universität Tübingen, Germany.
Angerer
A
A
Braun
V
V
D001425:Bacterial Outer Membrane Proteins / Q000502:physiology*; D002352:Carrier Proteins / Q000502:physiology; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins; D005290:Ferric Compounds / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D026901:Membrane Transport Proteins; D011487:Protein Conformation; D012333:RNA, Messenger / Q000235:genetics; D011956:Receptors, Cell Surface; D012808:Sigma Factor; D014158:Transcription, Genetic
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C028589:FecA protein, E coli; C093541:FecR protein, E coli; D005290:Ferric Compounds; D026901:Membrane Transport Proteins; D012333:RNA, Messenger; D011956:Receptors, Cell Surface; D012808:Sigma Factor; C025314:ferric citrate