Suppression of Escherichia coli formate hydrogenlyase activity by trimethylamine N-oxide is due to drainage of the inducer formate.

@article{Abaibou1997SuppressionOE,
  title={Suppression of Escherichia coli formate hydrogenlyase activity by trimethylamine N-oxide is due to drainage of the inducer formate.},
  author={Hafid Abaibou and Gérard Giordano and Marie-Andr{\~A}{\textcopyright}e Mandrand-Berthelot},
  journal={Microbiology},
  year={1997},
  volume={143 ( Pt 8)},
  pages={
          2657-64
        }
}
The effect of the addition of trimethylamine N-oxide (TMAO) in the growth medium on Escherichia coli anaerobic fermentative and respiratory pathways was examined. Formate dehydrogenase H (FDH-H) activity was totally repressed by the addition of 40 mM TMAO, whereas the overall hydrogenase (HYD) activity was reduced by 25%. Accordingly, expression of lacZ operon fusions with the fdhF and hycB structural genes specifying FDH-H and HYD3 was reduced sevenfold and eightfold, respectively, leading to… 

Figures and Tables from this paper

Hydrogenase 3 but not hydrogenase 4 is major in hydrogen gas production by Escherichia coli formate hydrogenlyase at acidic pH and in the presence of external formate
TLDR
Results indicate that Hyd-3 has a major role in H2 production at acidic pH independently on the F0F1-ATPase, and that this production became insensitive either to N,N′-dicyclohexylcarbodiimide or to osmotic shock.
Anaerobic Formate and Hydrogen Metabolism.
TLDR
Clear evidence now exists indicating that Escherichia coli can mature Hyd enzymes differentially, depending on metal ion availability and the prevailing metabolic state.
In vivo role of FdhD and FdmE in formate metabolism in Pseudomonas putida: Redundancy and expression in the stationary phase.
TLDR
Results suggest that redundancy in formaldehyde/formate metabolism in P. putida extends to the proteins involved in maturation/location of formate dehydrogenase complexes.
On the function of the various quinone species in Escherichia coli
TLDR
It is demonstrated that demethylmenaquinone serves as an electron acceptor for oxidation of succinate to fumarate, and that all three quinol oxidases of E. coli accept electrons from this naphtoquinone derivative.
Formate protects stationary‐phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide
TLDR
It is reported here that specific organic acids protect stationary‐phase Escherichia coli and Salmonella cells from killing by a potent antimicrobial peptide derived from the human bactericidal/permeability‐increasing protein (BPI).
Four components of the conjugated redox system in organisms: Carbon, nitrogen, sulfur, oxygen
TLDR
A model of a three-component conjugated redox system is proposed in which the methyl group oxidation pathway is an archaic and conservative donor of protons and electrons, the reduction of O2 serves as an acceptor, and the arginine amino group is used for production of both urea and nitric oxide.
Genomic Analysis of Family UBA6911 (Group 18 Acidobacteria) Expands the Metabolic Capacities of the Phylum and Highlights Adaptations to Terrestrial Habitats
TLDR
Genetic characterization of genomes belonging to family UBA6911 suggested that members of Acidobacteria group 18 are metabolically versatile heterotrophs capable of utilizing a wide range of proteins, amino acids, and sugars as carbon sources, possess respiratory and fermentative capacities, and display few auxotrophies.
Rates of DNA Sequence Evolution in Experimental Populations of Escherichia coli During 20,000 Generations
TLDR
The challenge of finding sequence variation among bacterial isolates that share such a recent ancestor provides a useful baseline for research aimed at finding the beneficial substitutions in these populations, and the number of synonymous substitutions is higher than predicted from measured mutation rates in E. coli.

References

SHOWING 1-10 OF 57 REFERENCES
Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase
TLDR
Aerobically expressed FDH-Z and NAR-Z enzymes were shown to reduce nitrate at the expense of formate under anaerobic conditions, suggesting that this pathway would allow the cell to respond quickly to anaerobiosis.
Identification of the formate dehydrogenases and genetic determinants of formate-dependent nitrite reduction by Escherichia coli K12.
TLDR
It is concluded that all three of the known formate dehydrogenases of E. coli can contribute to the transfer of electrons from formate to the Nrf pathway.
Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli
TLDR
An operon fusion between the dmsA gene, along with its associated regulatory region, and lacZ+ was constructed, establishing that the molybdenum ion but not the ability to form a functional cofactor is required for regulation of dmsABC.
Regulation of Escherichia coli fumarate reductase (frdABCD) operon expression by respiratory electron acceptors and the fnr gene product
TLDR
Nitrate repression of frdA'-'lacZ expression was observed under either aerobic or anaerobic cell growth conditions in both wild-type and fnr mutant strains, demonstrating that the mechanism for nitrate repression is independent of nitrate respiration and oxygen control imparted by Fnr.
Mechanism of regulation of the formate‐hydrogenlyase pathway by oxygen, nitrate, and pH: definition of the formate regulon
TLDR
Observations indicate that it is the intracellular level of formate that determines the transcription of the genes of the formate regulon by FhlA, a novel positive feedback mechanism in which the activator of a regulon induces its own synthesis in response to increases in the concentration of the catabolic substrate.
Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12.
TLDR
It is concluded that regulation of fdnGHI and narGHJI expression is mediated through common pathways.
Identification and expression of the Escherichia coli fdhD and fdhE genes, which are involved in the formation of respiratory formate dehydrogenase
TLDR
Initial experiments indicate that the region between the two genes seems not to be essential to FDH-PMS activity, which might suggest the participation of fdhE in the synthesis of the selenopolypeptide of FDH -PMS.
Hydrogen-dependent growth of Escherichia coli in anaerobic respiration and the presence of hydrogenases with different functions.
TLDR
E. coli K10 was found to grow anaerobically on molecular hydrogen by reducing nitrate, fumarate, and trimethylamine N-oxide when peptone was added to the culture medium, suggesting that multiple forms of hydrogenase are present.
...
...