ArticleJournal of bacteriology2003
Sites of interaction between the FecA and FecR signal transduction proteins of ferric citrate transport in Escherichia coli K-12.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 40 citations in OpenAlex.
- Cleavage cascade of the sigma regulator FecR orchestrates TonB-dependent signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bacterial TonB-dependent transducers interact with the anti-σ factor in absence of the inducing signal protecting it from proteolysis.PLoS biology · 2024Article
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- Transcription regulation of iron carrier transport genes by ECF sigma factors through signaling from the cell surface into the cytoplasm.FEMS microbiology reviews · 2022Article
- An Extracytoplasmic Function Sigma Factor Required for Full Virulence in Xanthomonas citri pv. citri.Journal of bacteriology · 2022Article
- Iron Transport and Metabolism in Escherichia, Shigella, and Salmonella.EcoSal Plus · 2021Article
- The quantitative basis for the redistribution of immobile bacterial lipoproteins to division septa.PLoS computational biology · 2021Article
- The multifarious roles of Tol-Pal in Gram-negative bacteria.FEMS microbiology reviews · 2020Review
- New Insights into the Regulation of Cell-Surface Signaling Activity Acquired from a Mutagenesis Screen of theFrontiers in microbiology · 2017Article
- Interaction of a partially disordered antisigma factor with its partner, the signaling domain of the TonB-dependent transporter HasR.PloS one · 2014Article
- Change is good: variations in common biological mechanisms in the epsilonproteobacterial genera Campylobacter and Helicobacter.Microbiology and molecular biology reviews : MMBR · 2011Review
- Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors.Biochimica et biophysica acta · 2008Review
- Signal transduction pathway of TonB-dependent transporters.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Transcriptional response of Escherichia coli to TPEN.Journal of bacteriology · 2006Article
- Residues involved in FecR binding are localized on one side of the FecA signaling domain in Escherichia coli.Journal of bacteriology · 2006Article
- Purification, crystallization and preliminary X-ray analysis of the outer membrane complex HasA-HasR from Serratia marcescens.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Bacterial metal detectors.Molecular microbiology · 2005Article
- Defined inactive FecA derivatives mutated in functional domains of the outer membrane transport and signaling protein of Escherichia coli K-12.Journal of bacteriology · 2004Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription of the fecABCDE ferric citrate transport genes of Escherichia coli K-12 is initiated by a signaling cascade from the cell surface into the cytoplasm. FecR receives the signal in the periplasm from the outer membrane protein FecA loaded with ferric citrate, transmits the signal across the cytoplasmic membrane, and converts FecI in the cytoplasm to an active sigma factor. In this study, it was shown through the use of a bacterial two-hybrid system that, in the periplasm, the C-terminal FecR(237-317) fragment interacts with the N-terminal FecA(1-79) fragment. In the same C-terminal region, amino acid residues important for the interaction of FecR with FecA were identified by random and site-directed mutagenesis. They were preferentially located in and around a leucine motif (residues 247 to 268) which was found to be highly conserved in FecR-like proteins. The degree of residual binding of FecR mutant proteins to FecA was correlated with the degree of transcription initiation in response to ferric citrate in the culture medium. Three randomly generated inactive FecR mutants, FecR(L254E), FecR(L269G), and FecR(F284L), were suppressed to different degrees by the mutants FecA(G39R) and FecR(D43E). One FecR mutant, FecR (D138E, V197A), induced fecA promoter-directed transcription constitutively in the absence of ferric citrate and bound more strongly than wild-type FecR to FecA. The data showed that FecR interacts in the periplasm with FecA to confer ferric citrate-induced transcription of the fec transport genes and identified sites in FecR and FecA that are important for signal transduction.
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