Import of Aspartate and Malate by DcuABC Drives H 2/Fumarate Respiration to Promote Salmonella Gut-Luminal Colonization

2019 ◽  
Author(s):  
Bidong D. Nguyen ◽  
Miguelangel Cuenca V. ◽  
Johannes Hartl ◽  
Rebekka Bauer ◽  
Susanne Meile ◽  
...  
Keyword(s):  
Fumarate Respiration

scholarly journals Import of Aspartate and Malate by DcuABC Drives H2/Fumarate Respiration to Promote Initial Salmonella Gut-Lumen Colonization in Mice

2020 ◽  
Vol 27 (6) ◽  
pp. 922-936.e6 ◽  
Author(s):  
Bidong D. Nguyen ◽  
Miguelangel Cuenca V. ◽  
Johannes Hartl ◽  
Ersin Gül ◽  
Rebekka Bauer ◽  
...  
Keyword(s):  
Fumarate Respiration

scholarly journals Salipiger mucescens gen. nov., sp. nov., a moderately halophilic, exopolysaccharide-producing bacterium isolated from hypersaline soil, belonging to the α-Proteobacteria

2004 ◽  
Vol 54 (5) ◽  
pp. 1735-1740 ◽  
Author(s):  
M. José Martínez-Cánovas ◽  
Emilia Quesada ◽  
Fernando Martínez-Checa ◽  
Ana del Moral ◽  
Victoria Béjar
Keyword(s):  
New Genus ◽  
Phylogenetic Analyses ◽  
Major Fatty Acid ◽  
Strictly Aerobic ◽  
New Genus And Species ◽  
Anaerobic Conditions ◽  
Fatty Acid Component ◽  
Moderately Halophilic ◽  
Fumarate Respiration ◽  
Distinct Line

Salipiger mucescens gen. nov., sp. nov. is a moderately halophilic, exopolysaccharide-producing, Gram-negative rod isolated from a hypersaline habitat in Murcia in south-eastern Spain. The bacterium is chemoheterotrophic and strictly aerobic (i.e. unable to grow under anaerobic conditions either by fermentation or by nitrate or fumarate respiration). It does not synthesize bacteriochlorophyll a. Catalase and phosphatase are positive. It does not produce acids from carbohydrates. It cannot grow with carbohydrates or amino acids as sole sources of carbon and energy. It grows best at 9–10 % w/v NaCl and requires the presence of Na+ but not Mg2+ or K+, although they do stimulate its growth somewhat when present. Its major fatty-acid component is 18 : 1ω7c (78·0 %). The predominant respiratory lipoquinone found in strain A3T is ubiquinone with ten isoprene units. The G+C content is 64·5 mol%. Phylogenetic analyses strongly indicate that this strain forms a distinct line within a clade containing the genus Roseivivax in the subclass α-Proteobacteria. The similarity value with Roseivivax halodurans and Roseivivax halotolerans is 94 %. In the light of the polyphasic evidence gathered in this study it is proposed that the isolate be classified as representing a new genus and species, Salipiger mucescens gen. nov., sp. nov. The proposed type strain is strain A3T (=CECT 5855T=LMG 22090T=DSM 16094T).

scholarly journals Regulation of tartrate metabolism by TtdR and relation to the DcuS–DcuR-regulated C4-dicarboxylate metabolism of Escherichia coli

Microbiology ◽  
2009 ◽  
Vol 155 (11) ◽  
pp. 3632-3640 ◽  
Author(s):  
Ok Bin Kim ◽  
Julia Reimann ◽  
Hanna Lukas ◽  
Uwe Schumacher ◽  
Jan Grimpo ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Promoter Region ◽  
Anaerobic Conditions ◽  
Two Component System ◽  
Two Component ◽  
Fumarate Respiration ◽  
Mutual Regulation ◽  
Genes Encoding ◽  
Type Gene ◽  
Tartrate Dehydratase

Escherichia coli catabolizes l-tartrate under anaerobic conditions to oxaloacetate by the use of l-tartrate/succinate antiporter TtdT and l-tartrate dehydratase TtdAB. Subsequently, l-malate is channelled into fumarate respiration and degraded to succinate by the use of fumarase FumB and fumarate reductase FrdABCD. The genes encoding the latter pathway (dcuB, fumB and frdABCD) are transcriptionally activated by the DcuS–DcuR two-component system. Expression of the l-tartrate-specific ttdABT operon encoding TtdAB and TtdT was stimulated by the LysR-type gene regulator TtdR in the presence of l- and meso-tartrate, and repressed by O2 and nitrate. Anaerobic expression required a functional fnr gene, and nitrate repression depended on NarL and NarP. Expression of ttdR, encoding TtdR, was repressed by O2, nitrate and glucose, and positively regulated by TtdR and DcuS. Purified TtdR specifically bound to the ttdR–ttdA promoter region. TtdR was also required for full expression of the DcuS–DcuR-dependent dcuB gene in the presence of tartrate. Overall, expression of the ttdABT genes is subject to l-/meso-tartrate-dependent induction, and to aerobic and nitrate repression. The control is exerted directly at ttdA and in addition indirectly by regulating TtdR levels. TtdR recognizes a subgroup (l- and meso-tartrate) of the stimuli perceived by the sensor DcuS, which responds to all C4-dicarboxylates; both systems apparently communicate by mutual regulation of the regulatory genes.

scholarly journals Succinate dehydrogenase functioning by a reverse redox loop mechanism and fumarate reductase in sulphate-reducing bacteria

Microbiology ◽  
2006 ◽  
Vol 152 (8) ◽  
pp. 2443-2453 ◽  
Author(s):  
Tanja Zaunmüller ◽  
David J. Kelly ◽  
Frank O. Glöckner ◽  
Gottfried Unden
Keyword(s):  
Succinate Dehydrogenase ◽  
Draft Genome ◽  
Desulfovibrio Desulfuricans ◽  
Geobacter Sulfurreducens ◽  
Fumarate Reductase ◽  
Desulfovibrio Vulgaris ◽  
Succinate Oxidation ◽  
Proton Potential ◽  
Fumarate Respiration ◽  
Reducing Bacteria

Sulphate- or sulphur-reducing bacteria with known or draft genome sequences (Desulfovibrio vulgaris, Desulfovibrio desulfuricans G20, Desulfobacterium autotrophicum [draft], Desulfotalea psychrophila and Geobacter sulfurreducens) all contain sdhCAB or frdCAB gene clusters encoding succinate : quinone oxidoreductases. frdD or sdhD genes are missing. The presence and function of succinate dehydrogenase versus fumarate reductase was studied. Desulfovibrio desulfuricans (strain Essex 6) grew by fumarate respiration or by fumarate disproportionation, and contained fumarate reductase activity. Desulfovibrio vulgaris lacked fumarate respiration and contained succinate dehydrogenase activity. Succinate oxidation by the menaquinone analogue 2,3-dimethyl-1,4-naphthoquinone depended on a proton potential, and the activity was lost after degradation of the proton potential. The membrane anchor SdhC contains four conserved His residues which are known as the ligands for two haem B residues. The properties are very similar to succinate dehydrogenase of the Gram-positive (menaquinone-containing) Bacillus subtilis, which uses a reverse redox loop mechanism in succinate : menaquinone reduction. It is concluded that succinate dehydrogenases from menaquinone-containing bacteria generally require a proton potential to drive the endergonic succinate oxidation. Sequence comparison shows that the SdhC subunit of this type lacks a Glu residue in transmembrane helix IV, which is part of the uncoupling E-pathway in most non-electrogenic FrdABC enzymes.

scholarly journals The effect of fumarate on respiration

1936 ◽  
Vol 121 (823) ◽  
pp. 338-357 ◽  
Keyword(s):  
Carbon Atom ◽  
Recent Work ◽  
Muscle Tissue ◽  
Cellular Respiration ◽  
Reversible System ◽  
Fundamental Function ◽  
Fumarate Respiration ◽  
Through Diffusion ◽  
Normal Respiration

The recent work of Szent-Gyorgyi and his co-workers (Gozsy and Szent-Gyorgyi, 1934; Annau et al .,1935) on the importance of fumarate in cellular respiration assigns a definite and fundamental function to the di-carboxylic four-carbon-atom acids and to the enzymes which activate them. Essentially their view is as follows: the reversible system, fumarate-oxalacetate, functions catalytically in transporting activated hydrogen from the metabolite dehydrogenation systems to the cytochrome (Warburg-Keilin) system through the medium of an intermediary substance. The oxalacetate formed takes up hydrogen, going either to fumarate, or to succinate by “ over-reduction ”. The succinate thus formed is converted to fumarate by means of succinodehydrogenase, and the catalytic cycle is completed. Malonate is known to inhibit succinodehydrogenase (Quastel and Wooldridge, 1928), and malonate also inhibits respiration. SzentGyorgyi et al . explain this inhibition by the fact that the succinate normally formed is prevented by malonate from being oxidized to fumarate, and respiration fails owing to a lack of fumarate. They further attribute the decrease in respiration of muscle tissue in vitro to a loss of fumarate through diffusion. If, however, this loss is compensated for by the addition of fresh fumarate, respiration proceeds normally. The addition of fumarate therefore “ preserves ” the normal respiration of the tissue.

C4-dicarboxylates as growth substrates and signaling molecules for commensal and pathogenic enteric bacteria in mammalian intestine

2022 ◽  
Author(s):  
Christopher Schubert ◽  
Gottfried Unden
Keyword(s):  
Nitrogen Assimilation ◽  
Enteric Bacteria ◽  
Signaling Molecules ◽  
Initial Growth ◽  
Signaling Molecule ◽  
E Coli ◽  
Fumarate Respiration ◽  
Net Uptake ◽  
Redox Shuttle ◽  
Mammalian Intestine

The C4-dicarboxylates (C4-DC) L-aspartate and L-malate have been identified as playing an important role in the colonization of mammalian intestine by enteric bacteria, such as Escherichia coli and Salmonella Typhimurium, and succinate as a signaling molecule for host–enteric bacteria interaction. Thus, endogenous and exogenous fumarate respiration and related functions are required for efficient initial growth of the bacteria. L-aspartate represents a major substrate for fumarate respiration in the intestine and a high-quality substrate for nitrogen assimilation. During nitrogen assimilation, DcuA catalyzes an L-aspartate/fumarate antiport and serves as a nitrogen shuttle for the net uptake of ammonium only, whereas DcuB acts as a redox shuttle that catalyzes the L-malate/succinate antiport during fumarate respiration. The C4-DC two-component system DcuS-DcuR is active in the intestine and responds to intestinal C4-DC levels. Moreover, in macrophages and in mice, succinate is a signal that promotes virulence and survival of S . Tm and pathogenic E. coli . On the other hand, intestinal succinate is an important signaling molecule for the host and activates response and protective programs. Therefore, C4-DCs play a major role in supporting colonization of enteric bacteria and as signaling molecules for the adaptation of host physiology.

scholarly journals C4-dicarboxylate metabolons: Interaction of C4-dicarboxylate transporters of Escherichia coli with cytosolic enzymes and regulators

2021 ◽  
Author(s):  
Christopher Schubert ◽  
Gottfried Unden
Keyword(s):  
Escherichia Coli ◽  
Nitrogen Assimilation ◽  
Concerted Action ◽  
Phosphotransferase System ◽  
Regulatory Pathways ◽  
E Coli ◽  
Fumarate Respiration ◽  
Genes Encoding ◽  
Two Hybrid

Metabolons represent the structural organization of proteins for metabolic or regulatory pathways. Here the interaction of enzymes fumarase FumB and aspartase AspA with the C4-DC transporters DcuA and DcuB of Escherichia coli was tested by a bacterial two-hybrid (BACTH) assay in situ, or by co-chromatography (mSPINE). DcuB interacted strongly with FumB and AspA, and DcuA with AspA. The fumB-dcuB and the dcuA-aspA genes encoding the respective proteins are known for their colocalization on the genome and the production of co-transcripts. The data consistently suggest the formation of DcuB/FumB, DcuB/AspA and DcuA/AspA metabolons in fumarate respiration for the uptake of L-malate, or L-aspartate, conversion to fumarate and excretion of succinate after reduction. The DcuA/AspA metabolon catalyzes L-Asp uptake and fumarate excretion in concerted action also to provide ammonia for nitrogen assimilation. The aerobic C4-DC transporter DctA interacted with the regulator EIIAGlc of the E. coli glucose phosphotransferase system. It is suggested that EIIAGlc inhibits C4-DC uptake by DctA in the presence of the preferred substrate glucose.

scholarly journals Structural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria

2015 ◽  
Vol 16 (12) ◽  
pp. 15287-15308 ◽  
Author(s):  
Daniel Inaoka ◽  
Tomoo Shiba ◽  
Dan Sato ◽  
Emmanuel Balogun ◽  
Tsuyoshi Sasaki ◽  
...  
Keyword(s):  
Molecular Design ◽  
Fumarate Respiration ◽  
Structural Insights

scholarly journals Transport of C4-Dicarboxylates inWolinella succinogenes

2000 ◽  
Vol 182 (20) ◽  
pp. 5757-5764 ◽  
Author(s):  
Roland Ullmann ◽  
Roland Gross ◽  
Jörg Simon ◽  
Gottfried Unden ◽  
Achim Kröger
Keyword(s):  
Carbon Source ◽  
Cytoplasmic Membrane ◽  
Anaerobic Respiration ◽  
Molar Ratio ◽  
Nitrate Respiration ◽  
Gene Products ◽  
Dicarboxylate Transport ◽  
Proton Potential ◽  
Fumarate Respiration ◽  
Cytoplasmic Side

ABSTRACT C4-dicarboxylate transport is a prerequisite for anaerobic respiration with fumarate in Wolinella succinogenes, since the substrate site of fumarate reductase is oriented towards the cytoplasmic side of the membrane. W. succinogenes was found to transport C4-dicarboxylates (fumarate, succinate, malate, and aspartate) across the cytoplasmic membrane by antiport and uniport mechanisms. The electrogenic uniport resulted in dicarboxylate accumulation driven by anaerobic respiration. The molar ratio of internal to external dicarboxylate concentration was up to 103. The dicarboxylate antiport was either electrogenic or electroneutral. The electroneutral antiport required the presence of internal Na+, whereas the electrogenic antiport also operated in the absence of Na+. In the absence of Na+, no electrochemical proton potential (Δp) was measured across the membrane of cells catalyzing fumarate respiration. This suggests that the proton potential generated by fumarate respiration is dissipated by the concomitant electrogenic dicarboxylate antiport. Three gene loci (dcuA,dcuB, and dctPQM) encoding putative C4-dicarboxylate transporters were identified on the genome of W. succinogenes. The predicted gene products ofdcuA and dcuB are similar to the Dcu transporters that are involved in the fumarate respiration ofEscherichia coli with external C4-dicarboxylates. The genes dctP, -Q, and -M probably encode a binding-protein-dependent secondary uptake transporter for dicarboxylates. A mutant (DcuA− DcuB−) ofW. succinogenes lacking the intact dcuA anddcuB genes grew by nitrate respiration with succinate as the carbon source but did not grow by fumarate respiration with fumarate, malate, or aspartate as substrates. The DcuA−, DcuB−, and DctQM− mutants grew by fumarate respiration as well as by nitrate respiration with succinate as the carbon source. Cells of the DcuA− DcuB−mutant performed fumarate respiration without generating a proton potential even in the presence of Na+. This explains why the DcuA− DcuB− mutant does not grow by fumarate respiration. Growth by fumarate respiration appears to depend on the function of the Na+-dependent, electroneutral dicarboxylate antiport which is catalyzed exclusively by the Dcu transporters. Dicarboxylate transport via the electrogenic uniport is probably catalyzed by the DctPQM transporter and by a fourth, unknown transporter that may also operate as an electrogenic antiporter.

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