Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase

@article{Abaibou1995ExpressionAC,
  title={Expression and characterization of the Escherichia coli fdo locus and a possible physiological role for aerobic formate dehydrogenase},
  author={Hafid Abaibou and Janine Pommier and S Benoit and Gérard Giordano and Marie-Andr{\~A}{\textcopyright}e Mandrand-Berthelot},
  journal={Journal of Bacteriology},
  year={1995},
  volume={177},
  pages={7141 - 7149}
}
In the presence of nitrate, the major anaerobic respiratory pathway includes formate dehydrogenase (FDH-N) and nitrate reductase (NAR-A), which catalyze formate oxidation coupled to nitrate reduction. Two aerobically expressed isoenzymes, FDH-Z and NAR-Z, have been recently characterized. Enzymatic analysis of plasmid subclones carrying min 88 of the Escherichia coli chromosome was consistent with the location of the fdo locus encoding FDH-Z between the fdhD and fdhE genes which are necessary… 
View on ASMUSA
ncbi.nlm.nih.gov
85 Citations
Highly Influential Citations
9
Background Citations
41
Methods Citations
2
Results Citations
2

85 Citations

Biosynthesis of the respiratory formate dehydrogenases from Escherichia coli: characterization of the FdhE protein
TLDR
It is shown that E. coli FdhE interacts with the catalytic subunits of the respiratory formate dehydrogenases, and site-directed mutagenesis shows that conserved cysteine motifs are essential for the physiological activity of the Fdh E protein and are also involved in iron ligation.
Coordinate Regulation of the Escherichia coli Formate Dehydrogenase fdnGHI and fdhF Genes in Response to Nitrate, Nitrite, and Formate: Roles for NarL and NarP
TLDR
The different gene expression profiles of the alternative formate dehydrogenase operons suggest that the two enzymes have complementary physiological roles under environmental conditions when nitrate and formate levels are changing.
Suppression of Escherichia coli formate hydrogenlyase activity by trimethylamine N-oxide is due to drainage of the inducer formate.
TLDR
Results strongly suggest that formate-dependent reduction of TMAO via FDH-N and TOR reduces the amount of formate available for induction of the formate hydrogenlyase pathway.
Topological Analysis of the Aerobic Membrane-Bound Formate Dehydrogenase of Escherichia coli
TLDR
It is suggested that the alphabeta catalytic dimer is located in the cytoplasm, with a C-terminal anchor for beta protruding into the periplasm, in contrast to previously reported predictions from sequence analysis.
Involvement of formate dehydrogenases in stationary phase oxidative stress tolerance in Escherichia coli
TLDR
It is suggested that formate dehydrogenase‐O serves as an electron transfer element in glucose metabolism to promote oxidative stress tolerance and survival in stationary phase.
Structural Analysis of the fds Operon Encoding the NAD+-linked Formate Dehydrogenase of Ralstonia eutropha *
TLDR
It is proposed that the NH2-terminal domain of FdsA together with FdsB and FdsG constitute a functional entity corresponding to the NADH dehydrogenase (diaphorase) part of NADH:ubiquinone oxidoreductase and the hydrogenases.
Mapping cell envelope and periplasm protein interactions of Escherichia coli respiratory formate dehydrogenases by chemical cross-linking and mass spectrometry.
TLDR
This work presents for the first time the identification of cell envelope interaction partners of Fdh-N and -O from anaerobically grown E. coli using a heterobifunctional amine/photo-reactive cross-linker and mass spectrometric analysis of the cross-linked products.
Expression systems for soluble metal-dependent formate dehydrogenase
A-Type Carrier Protein ErpA Is Essential for Formation of an Active Formate-Nitrate Respiratory Pathway in Escherichia coli K-12
TLDR
The findings suggest that ErpA and IscA have overlapping roles in assembly of these anaerobic respiratory enzymes but demonstrate that ErPA is essential for the production of active enzymes.
Model-assisted formate dehydrogenase-O (fdoH) gene knockout for enhanced succinate production in Escherichia coli from glucose and glycerol carbon sources
TLDR
It is revealed that a single deletion of the fdoH gene is sufficient to increase succinate production in E. coli from both glucose and glycerol substrates.
...
...

References

SHOWING 1-10 OF 59 REFERENCES
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.
Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12
TLDR
These complementation tests indicate that the S. typhimurium fdnC and fdnB genes are functionally homologous to the E. coli fdhD and fdhE genes, respectively, indicating that the rha-linked Salmonella typhIMurium genes are required primarily for formate dehydrogenase-N activity.
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.
The identification of mutants of Escherichia coli deficient in formate dehydrogenase and nitrate reductase activities using dye indicator plates
TLDR
A detailed analysis of the molecular genetics of the Escherichia coli system is begun with particular emphasis on firstly the unambiguous characterizations of the products of the various structural genes so far described, and secondly the identification of the regulatory genes responsible for the control of structural gene expression.
A second phenazine methosulphate-linked formate dehydrogenase isoenzyme in Escherichia coli.
Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) encodes selenocysteine.
Mutants of Escherichia coli specifically deficient in respiratory formate dehydrogenase activity.
TLDR
Construction of merodiploid strains harbouring various combinations of the mutated alleles, fdhE on the episome and fdhD on the chromosome, led to the restoration of FDH-PMS activity by complementation of the products encoded by the respective wild-type alleles.
Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme
TLDR
A detailed analysis of the expression of the sel genes showed that transcription was constitutive, being influenced neither by aerobiosis or anaerobiosis nor by the intracellular selenium concentration, and it is probable that this selenopolypeptide constitutes a major component of the formate oxidase.
Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity.
...
...