C4-dicarboxylate carriers and sensors in bacteria

Janausch, Ingo G.; Zientz, E.; Tran, Quang Hon; Kröger, Achim; Unden, Gottfried

doi:10.1016/s0005-2728(01)00233-x

Cited by 233 publications

(268 citation statements)

References 87 publications

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“…DcuB is predicted to function as a transporter for C 4 -dicarboxylates (succinate and fumarate), exchanging succinate for fumarate, which serves as a terminal electron acceptor (37). It should be pointed out that DcuA and DcuB in E. coli have overlapping functions and that both can transport succinate, fumarate, malate, and aspartate (15). The Cj0264c protein is the sole dimethyl sulfoxide (DMSO)/trimethylamine oxide (TMAO) reductase in C. jejuni and was shown by Sellars et al (37) to support DMSO-or TMAO-dependent growth under oxygen-limited conditions.…”

Section: Discussionmentioning

confidence: 99%

CmeR Functions as a Pleiotropic Regulator and Is Required for Optimal Colonization of Campylobacter jejuni In Vivo

Guo¹,

Wang²,

Shi³

et al. 2008

J Bacteriol

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Section: Discussionmentioning

confidence: 99%

CmeR Functions as a Pleiotropic Regulator and Is Required for Optimal Colonization of Campylobacter jejuni In Vivo

Guo¹,

Wang²,

Shi³

et al. 2008

J Bacteriol

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“…DcuS-DcuR is a twocomponent system consisting of the sensor kinase DcuS and the response regulator DcuR (Golby et al, 1999;Janausch et al, 2002;Zientz et al, 1998). DcuS-DcuR controls the expression of genes for the 'general' C 4 -dicarboxylate metabolism, such as dcuB, fumB and frdABCD.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2009

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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 LysRtype gene regulator TtdR in the presence of L-and meso-tartrate, and repressed by O 2 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 O 2 , 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-tartratedependent 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 mesotartrate) of the stimuli perceived by the sensor DcuS, which responds to all C 4 -dicarboxylates; both systems apparently communicate by mutual regulation of the regulatory genes.

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“…The sensor kinase DcuS is a member of the CitA family of histidine kinases, and it responds to C 4 -dicarboxylates such as fumarate, succinate, malate, and tartrate (5,7). Upon detection of its cognate ligand, the DcuS-DcuR system up-regulates the synthesis of both fumarate reductase (frdABCD) and also the anaerobic fumarate-succinate antiporter DcuB.…”

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confidence: 99%

“…The response regulator DctD controls the expression of the dicarboxylate transporter DctA, another integral membrane protein (10). Studies have shown that either the ligand specificity or the signaling state of DctB may be modified by DctA, through a possible direct interaction between DctA and DctB (7,11). The DctB ortholog in Vibrio cholerae is the product of gene VC1925, a protein annotated in the Swiss-PROT/ TrEMBL (13) data base as a putative histidine kinase sensor under accession number Q9KQS3.…”

mentioning

confidence: 99%

“…The DctB ortholog in Vibrio cholerae is the product of gene VC1925, a protein annotated in the Swiss-PROT/ TrEMBL (13) data base as a putative histidine kinase sensor under accession number Q9KQS3. It shows high sequence similarity to the previously studied rhizobial DctB sensors, and it has been grouped into the NtrB C 4 -dicarboxylate sensor histidine kinase family (7). The exact function of DctB in V. cholerae has yet to be determined.…”

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confidence: 99%

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Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB

Cheung

Hendrickson

2008

Journal of Biological Chemistry

102

161

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Two-component signaling systems allow bacteria to adapt to changing environments. Typically, a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane in histidine kinases are not fully understood. In an effort to further understand such processes, we have solved the crystal structures of the periplasmic sensor domains of Escherichia coli DcuS and of Vibrio cholerae DctB in complex with the respective cognate ligands, malate and succinate. Both proteins are involved in the regulation of the transport and metabolism of C 4 -dicarboxylates, but they are not highly related by sequence similarity. Our work reveals that despite disparate sizes, both structures contain a similar characteristic ␣/␤ PDC (PhoQ-DcuS-CitA) sensor-domain fold and display similar modes of ligand binding, suggesting similar mechanisms of function.The ability of bacteria to monitor and adapt to their environment is crucial to their survival, and two-component signal transduction systems mediate most of these adaptive responses. One component is a histidine kinase sensor, most commonly part of a homodimeric transmembrane sensor protein, and the second component is a cytoplasmic response regulator. The two components interact in tandem through a phosphotransfer cascade (1-4). A typical transmembrane sensor protein contains a periplasmic sensor domain and a cytoplasmic histidine kinase domain. Upon binding of a ligand to the periplasmic sensor domain, this signal is transduced across the membrane to the cytoplasmic domain where an ATP-dependent autophosphorylation of a conserved histidine residue occurs (1). The phosphate is subsequently transferred to a conserved aspartate residue in the response regulator protein by an auto-catalyzed reaction (2), ultimately leading to adaptive modulation of gene expression. In some circumstances, sensor stimulation leads to dephosphorylation. Within the large family of protein histidine kinases, the sequence of the sensor domain is considered to be modular, whereas that of the histidine kinase domain is more conserved. Over the past decade, especially with the determination of numerous bacterial genome sequences, hundreds of new histidine kinase proteins have been identified but remain unstudied.The DcuS-DcuR two component system is involved in the regulation of the anaerobic fumarate respiratory pathway in Escherichia coli (5, 6). The sensor kinase DcuS is a member of the CitA family of histidine kinases, and it responds to C 4 -dicarboxylates such as fumarate, succinate, malate, and tartrate (5, 7). Upon detection of its cognate ligand, the DcuS-DcuR system up-regulates the synthesis of both fumarate reductase (frdABCD) and also the anaerobic fumarate-succinate antiporter DcuB. DcuS is p...

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C4-dicarboxylate carriers and sensors in bacteria

Cited by 233 publications

References 87 publications

CmeR Functions as a Pleiotropic Regulator and Is Required for Optimal Colonization of Campylobacter jejuni In Vivo

CmeR Functions as a Pleiotropic Regulator and Is Required for Optimal Colonization of Campylobacter jejuni In Vivo

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

Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB

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