6533b7dafe1ef96bd126ee6a
RESEARCH PRODUCT
O2-sensing and O2-dependent gene regulation in facultatively anaerobic bacteria.
Sabine BeckerJohannes BongaertsG. HolighausJan SchirawskiGottfried UndenS. Sixsubject
Iron-Sulfur ProteinsGram-Negative Facultatively Anaerobic RodsAnaerobic respirationRegulatorBiologymedicine.disease_causeBiochemistryMicrobiologychemistry.chemical_compoundBacterial ProteinsGeneticsmedicineMolecular BiologyHemeEscherichia coliRegulation of gene expressionSensory mechanismEscherichia coli ProteinsGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationOxygenchemistryBiochemistrybacteriaAnaerobic bacteriaBacteriaTranscription Factorsdescription
Availability of O2 is one of the most important regulatory signals in facultatively anaerobic bacteria. Various two- or one-component sensor/regulator systems control the expression of aerobic and anaerobic metabolism in response to O2. Most of the sensor proteins contain heme or Fe as cofactors that interact with O2 either by binding or by a redox reaction. The ArcA/ArcB regulator of aerobic metabolism in Escherichia coli may use a different sensory mechanism. In two-component regulators, the sensor is located in the cytoplasmic membrane, whereas one-component regulators are located in the cytoplasm. Under most conditions, O2 can readily reach the cytoplasm and could provide the signal in the cytoplasm. The transcriptional regulator FNR of E. coli controls the expression of many genes required for anaerobic metabolism in response to O2. Functional homologs of FNR are present in facultatively anaerobic Proteobacteria and presumably also in gram-positive bacteria. The target genes of FNR are mostly under multiple regulation by FNR and other regulators that respond to O2, nitrate, or glucose. FNR represents a ’one-component' sensor/regulator and contains Fe for signal perception. In response to O2 availability, FNR is converted reversibly from the aerobic (inactive) state to the anaerobic (active) state. Experiments suggest that the Fe cofactor is bound by four essential cysteine residues. The O2-triggered transformation between active and inactive FNR presumably is due to a redox reaction at the Fe cofactor, but other modes of interaction cannot be excluded. O2 seems to affect the site-specific DNA binding of FNR at target genes or the formation of an active transcriptional complex with RNA polymerase.
year | journal | country | edition | language |
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1995-08-01 | Archives of microbiology |