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Journal articles on the topic 'KdpFABCQ'

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Published: 4 June 2021
Last updated: 1 February 2022

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1

Bertrand, Jessica, Karlheinz Altendorf, and Marc Bramkamp. "Amino Acid Substitutions in Putative Selectivity Filter Regions III and IV in KdpA Alter Ion Selectivity of the KdpFABC Complex from Escherichia coli." Journal of Bacteriology 186, no. 16 (2004): 5519–22. http://dx.doi.org/10.1128/jb.186.16.5519-5522.2004.

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ABSTRACT When grown under conditions of potassium limitation or high osmolality, Escherichia coli synthesizes the K+-translocating KdpFABC complex. The KdpA subunit, which has sequence homology to potassium channels of the KcsA type, has been shown to be important for potassium binding and transport. Replacement of the glycine residues in KdpA at positions 345 and 470, members of putative selectivity filter regions III and IV, alters the ion selectivity of the KdpFABC complex.
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2

Zimmann, Petra, Anne Steinbrügge, Maren Schniederberend, Kirsten Jung, and Karlheinz Altendorf. "The Extension of the Fourth Transmembrane Helix of the Sensor Kinase KdpD of Escherichia coli Is Involved in Sensing." Journal of Bacteriology 189, no. 20 (2007): 7326–34. http://dx.doi.org/10.1128/jb.00976-07.

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ABSTRACT The KdpD sensor kinase and the KdpE response regulator control expression of the kdpFABC operon coding for the KdpFABC high-affinity K+ transport system of Escherichia coli. In search of a distinct part of the input domain of KdpD which is solely responsible for K+ sensing, sequences of kdpD encoding the transmembrane region and adjacent N-terminal and C-terminal extensions were subjected to random mutagenesis. Nine KdpD derivatives were identified that had lost tight regulation of kdpFABC expression. They all carried single amino acid replacements located in a region encompassing the fourth transmembrane helix and the adjacent arginine cluster of KdpD. All mutants exhibited high levels of kdpFABC expression regardless of the external K+ concentration. However, 3- to 14-fold induction was observed under extreme K+-limiting conditions and in response to an osmotic upshift when sucrose was used as an osmolyte. These KdpD derivatives were characterized by a reduced phosphatase activity in comparison to the autokinase activity in vitro, which explains constitutive expression. Whereas for wild-type KdpD the autokinase activity and also, in turn, the phosphotransfer activity to KdpE were inhibited by increasing concentrations of K+, both activities were unaffected in the KdpD derivatives. These data clearly show that the extension of the fourth transmembrane helix encompassing the arginine cluster is mainly involved in sensing both K+ limitation and osmotic upshift, which may not be separated mechanistically.
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3

Wolf, S., K. Pflüger-Grau, and A. Kremling. "Modeling the Interplay of Pseudomonas putida EIIANtr with the Potassium Transporter KdpFABC." Journal of Molecular Microbiology and Biotechnology 25, no. 2-3 (2015): 178–94. http://dx.doi.org/10.1159/000381214.

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The nitrogen phosphotransferase system (PTS<sup>Ntr</sup>) of <i>Pseudomonas putida</i> is a key regulatory device that participates in controlling many physiological processes in a posttranscriptional fashion. One of the target functions of the PTS<sup>Ntr</sup> is the regulation of potassium transport. This is mediated by the direct interaction of one of its components with the sensor kinase KdpD of the two-component system controlling transcription of the <i>kdpFABC</i> genes. From a detailed experimental analysis of the activity of the <i>kdpF</i> promoter in <i>P. putida</i> wild-type and <i>pts</i> mutant strains with varying potassium concentrations, we had highly time-resolved data at hand, describing the influence of the PTS<sup>Ntr</sup> on the transcription of the KdpFABC potassium transporter. Here, this data was used to construct a mathematical model based on a black box approach. The model was able to describe the data quantitatively with convincing accuracy. The qualitative interpretation of the model allowed the prediction of two general points describing the interplay between the PTS<sup>Ntr</sup> and the KdpFABC potassium transporter: (1) the influence of cell number on the performance of the <i>kdpF</i> promoter is mainly by dilution by growth and (2) potassium uptake is regulated not only by the activity of the KdpD/KdpE two-component system (in turn influenced by PtsN). An additional controller with integrative behavior is predicted by the model structure. This suggests the presence of a novel physiological mechanism during regulation of potassium uptake with the KdpFABC transporter and may serve as a starting point for further investigations.
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4

van der Laan, Martin, Michael Gaßel, and Karlheinz Altendorf. "Characterization of Amino Acid Substitutions in KdpA, the K+-Binding and -Translocating Subunit of the KdpFABC Complex of Escherichia coli." Journal of Bacteriology 184, no. 19 (2002): 5491–94. http://dx.doi.org/10.1128/jb.184.19.5491-5494.2002.

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ABSTRACT When grown under K+ limitation, Escherichia coli induces the K+-translocating KdpFABC complex. The stimulation of ATPase activity by NH4 + ions was shown for the first time. Substitutions in KdpA, which is responsible for K+ binding and translocation, revealed that enzyme complexes KdpA:G232A and KdpA:G232S have completely lost their cation selectivity.
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5

Pedersen, Bjørn P., David L. Stokes, and Hans-Jürgen Apell. "The KdpFABC complex – K+transport against all odds." Molecular Membrane Biology 35, no. 1 (2019): 21–38. http://dx.doi.org/10.1080/09687688.2019.1638977.

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6

Ballal, Anand, Marc Bramkamp, Hema Rajaram, Petra Zimmann, Shree Kumar Apte, and Karlheinz Altendorf. "An Atypical KdpD Homologue from the Cyanobacterium Anabaena sp. Strain L-31: Cloning, In Vivo Expression, and Interaction with Escherichia coli KdpD-CTD." Journal of Bacteriology 187, no. 14 (2005): 4921–27. http://dx.doi.org/10.1128/jb.187.14.4921-4927.2005.

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ABSTRACT The kdpFABC operon of Escherichia coli, coding for the high-affinity K+ transport system KdpFABC, is transcriptionally regulated by the products of the adjacently located kdpDE genes. The KdpD protein is a membrane-bound sensor kinase consisting of a large N-terminal domain and a C-terminal transmitter domain interconnected by four transmembrane segments (the transmembrane segments together with the C-terminal transmitter domain of KdpD are referred to as CTD), while KdpE is a cytosolic response regulator. We have cloned and sequenced the kdp operon from a nitrogen-fixing, filamentous cyanobacterium, Anabaena sp. strain L-31 (GenBank accession. number AF213466 ). The kdpABC genes are similar in size to those of E. coli, but the kdpD gene is short (coding only for 365 amino acids), showing homology only to the N-terminal domain of E. coli KdpD. A kdpE-like gene is absent in the vicinity of this operon. Anabaena KdpD with six C-terminal histidines was overproduced in E. coli and purified by Ni2+-nitrilotriacetic acid affinity chromatography. With antisera raised against the purified Anabaena KdpD, the protein was detected in Anabaena sp. strain L-31 membranes. The membrane-associated or soluble form of the Anabaena KdpD(6His) could be photoaffinity labeled with the ATP analog 8-azido-ATP, indicating the presence of an ATP binding site. The coproduction of Anabaena KdpD with E. coli KdpD-CTD decreased E. coli kdpFABC expression in response to K+ limitation in vivo relative to the wild-type KdpD-CTD protein. In vitro experiments revealed that the kinase activity of the E. coli KdpD-CTD was unaffected, but its phosphatase activity increased in the presence of Anabaena KdpD(6His). To our knowledge this is the first report where a heterologous N-terminal domain (Anabaena KdpD) is shown to affect in trans KdpD-CTD (E. coli) activity, which is just opposite to that observed for the KdpD-N-terminal domain of E. coli.
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7

Huang, Ching-Shin, Bjørn Panyella Pedersen, and David L. Stokes. "Crystal structure of the potassium-importing KdpFABC membrane complex." Nature 546, no. 7660 (2017): 681–85. http://dx.doi.org/10.1038/nature22970.

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8

Sweet, Marie, Hediye Erdjument-Bromage, Thomas A. Neubert, and David L. Stokes. "Action and Inactivation of the Bacterial Potassium Pump KdpFABC." Biophysical Journal 118, no. 3 (2020): 18a. http://dx.doi.org/10.1016/j.bpj.2019.11.281.

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9

Sweet, Marie E., Casper Larsen, Xihui Zhang, Michael Schlame, Bjørn P. Pedersen, and David L. Stokes. "Structural basis for potassium transport in prokaryotes by KdpFABC." Proceedings of the National Academy of Sciences 118, no. 29 (2021): e2105195118. http://dx.doi.org/10.1073/pnas.2105195118.

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KdpFABC is an oligomeric K+ transport complex in prokaryotes that maintains ionic homeostasis under stress conditions. The complex comprises a channel-like subunit (KdpA) from the superfamily of K+ transporters and a pump-like subunit (KdpB) from the superfamily of P-type ATPases. Recent structural work has defined the architecture and generated contradictory hypotheses for the transport mechanism. Here, we use substrate analogs to stabilize four key intermediates in the reaction cycle and determine the corresponding structures by cryogenic electron microscopy. We find that KdpB undergoes conformational changes consistent with other representatives from the P-type superfamily, whereas KdpA, KdpC, and KdpF remain static. We observe a series of spherical densities that we assign as K+ or water and which define a pathway for K+ transport. This pathway runs through an intramembrane tunnel in KdpA and delivers ions to sites in the membrane domain of KdpB. Our structures suggest a mechanism where ATP hydrolysis is coupled to K+ transfer between alternative sites in KdpB, ultimately reaching a low-affinity site where a water-filled pathway allows release of K+ to the cytoplasm.
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10

Jung, Kirsten, Mechthild Krabusch, and Karlheinz Altendorf. "Cs+ Induces the kdpOperon of Escherichia coli by Lowering the Intracellular K+ Concentration." Journal of Bacteriology 183, no. 12 (2001): 3800–3803. http://dx.doi.org/10.1128/jb.183.12.3800-3803.2001.

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ABSTRACT Cs+ was found to induce expression of thekdpFABC operon, encoding a high-affinity K+uptake system of Escherichia coli. Quantitative expression analyses at the transcriptional and translational levels reveal that CsCl causes much higher induction of kdpFABCthan does NaCl. A decrease of the intracellular K+concentration is found in cells exposed to CsCl. The results indicate that kdpFABC expression is induced when the intracellular K+ concentration is lowered. Moreover, the results imply that the signal transduction cascade mediated by KdpD and KdpE is able to integrate multiple signals.
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11

Damnjanovic, Bojana, Annemarie Weber, Meike Potschies, Jörg-Christian Greie, and Hans-Jürgen Apell. "Mechanistic Analysis of the Pump Cycle of the KdpFABC P-Type ATPase." Biochemistry 52, no. 33 (2013): 5563–76. http://dx.doi.org/10.1021/bi400729e.

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12

Gassel, Michael, and Karlheinz Altendorf. "Analysis of KdpC of the K+-transporting KdpFABC complex of Escherichia coli." European Journal of Biochemistry 268, no. 6 (2001): 1772–81. http://dx.doi.org/10.1046/j.1432-1033.2001.02048.x.

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13

Gaßel, Michael, and Karlheinz Altendorf. "Analysis of KdpC of the K+ -transporting KdpFABC complex of Escherichia coli." European Journal of Biochemistry 268, no. 6 (2001): 1772–81. http://dx.doi.org/10.1046/j.1432-1327.2001.02048.x.

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14

Hamann, Knut, Petra Zimmann, and Karlheinz Altendorf. "Reduction of Turgor Is Not the Stimulus for the Sensor Kinase KdpD of Escherichia coli." Journal of Bacteriology 190, no. 7 (2008): 2360–67. http://dx.doi.org/10.1128/jb.01635-07.

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ABSTRACT Stimulus perception by the KdpD/KdpE two-component system of Escherichia coli is still controversial with respect to the nature of the stimulus that is perceived by the sensor kinase KdpD. Limiting potassium concentrations in the medium or high osmolality leads to KdpD/KdpE signal transduction, resulting in kdpFABC expression. It has been hypothesized that changes in turgor are sensed by KdpD through alterations in the physical state of the cytoplasmic membrane. However, in this study the quantitative determination of expression levels of the kdpFABC operon revealed that the system responds very effectively to K+-limiting conditions in the medium but barely and to various degrees to salt and sugar stress. Since the current view of stimulus perception calls for mainly intracellular parameters, which might be sensed by KdpD, we set out to test the cytoplasmic concentrations of ATP, K+, Na+, glutamate, proline, glycine, trehalose, putrescine, and spermidine under K+-limiting conditions. As a first result, the determination of the cytoplasmic volume, which is a prerequisite for such measurements, revealed that a transient shrinkage of the cytoplasmic volume, which is indicative of a reduction in turgor, occurred only under osmotic upshift but not under K+-limiting conditions. Furthermore, the intracellular ATP concentration significantly increased under osmotic upshift, whereas only a slight increase occurred after a potassium downshift. Finally, the cytoplasmic K+ concentration rose severalfold only after an osmotic upshock. For the first time, these data indicate that stimulus perception by KdpD correlates neither with changes in the cytoplasmic volume nor with changes in the intracellular ATP or K+ concentration or those of the other solutes tested. In conclusion, we propose that a reduction in turgor cannot be the stimulus for KdpD.
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15

Damnjanovic, Bojana, and Hans-Jürgen Apell. "KdpFABC Reconstituted in Escherichia coli Lipid Vesicles: Substrate Dependence of the Transport Rate." Biochemistry 53, no. 35 (2014): 5674–82. http://dx.doi.org/10.1021/bi5008244.

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16

Kixmüller, Dorthe, Henrik Strahl, Andy Wende, and Jörg-Christian Greie. "Archaeal transcriptional regulation of the prokaryotic KdpFABC complex mediating K+ uptake in H. salinarum." Extremophiles 15, no. 6 (2011): 643–52. http://dx.doi.org/10.1007/s00792-011-0395-y.

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17

Stock, Charlott, Lisa Hielkema, Igor Tascon, et al. "The KdpFABC Complex: What Happens When a P-Type ATPase Hijacks an Ion Channel." Biophysical Journal 116, no. 3 (2019): 10a—11a. http://dx.doi.org/10.1016/j.bpj.2018.11.095.

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18

Lüttmann, Denise, Yvonne Göpel, and Boris Görke. "Cross-Talk between the Canonical and the Nitrogen-Related Phosphotransferase Systems Modulates Synthesis of the KdpFABC Potassium Transporter in Escherichia coli." Journal of Molecular Microbiology and Biotechnology 25, no. 2-3 (2015): 168–77. http://dx.doi.org/10.1159/000375497.

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Many Proteobacteria possess the regulatory nitrogen-related phosphotransferase system (PTS<sup>Ntr</sup>), which operates in parallel to the transport PTS. PTS<sup>Ntr</sup> is composed of the proteins EI<sup>Ntr</sup> and NPr and the final phosphate acceptor EIIA<sup>Ntr</sup>. Both PTSs can exchange phosphoryl groups among each other. Proteins governing K<sup>+</sup> uptake represent a major target of PTS<sup>Ntr</sup> in <i>Escherichia coli</i>. Nonphosphorylated EIIA<sup>Ntr</sup> binds and stimulates the K<sup>+</sup> sensor KdpD, which activates expression of the <i>kdpFABC</i> operon encoding a K<sup>+</sup> transporter. Here we show that this regulation also operates in an <i>ilvG</i><sup><i>+</i></sup> strain ruling out previous concern about interference with a nonfunctional <i>ilvG</i> allele present in many strains. Furthermore, we analyzed phosphorylation of EIIA<sup>Ntr</sup>. In wild-type cells EIIA<sup>Ntr</sup> is predominantly phosphorylated, regardless of the growth stage and the utilized carbon source. However, cross-phosphorylation of EIIA<sup>Ntr</sup> by the transport PTS becomes apparent in the absence of EI<sup>Ntr</sup>: EIIA<sup>Ntr</sup> is predominantly nonphosphorylated when cells grow on a PTS sugar and phosphorylated when a non-PTS carbohydrate is utilized. These differences in phosphorylation are transduced into corresponding <i>kdpFABC</i> transcription levels. Thus, the transport PTS may affect phosphorylation of EIIA<sup>Ntr</sup> and accordingly modulate processes controlled by EIIA<sup>Ntr</sup>. Our data suggest that this cross-talk becomes most relevant under conditions that would inhibit activity of EI<sup>Ntr</sup>.
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19

Xue, Ting, Yibo You, De Hong, Haipeng Sun, and Baolin Sun. "The Staphylococcus aureus KdpDE Two-Component System Couples Extracellular K+Sensing and Agr Signaling to Infection Programming." Infection and Immunity 79, no. 6 (2011): 2154–67. http://dx.doi.org/10.1128/iai.01180-10.

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ABSTRACTThe Kdp system is widely distributed among bacteria. InEscherichia coli, the Kdp-ATPase is a high-affinity K+uptake system and its expression is activated by the KdpDE two-component system in response to K+limitation or salt stress. However, information about the role of this system in many bacteria still remains obscure. Here we demonstrate that KdpFABC inStaphylococcus aureusis not a major K+transporter and that the main function of KdpDE is not associated with K+transport but that instead it regulates transcription for a series of virulence factors through sensing external K+concentrations, indicating that this bacterium might modulate its infectious status through sensing specific external K+stimuli in different environments. Our results further reveal thatS. aureusKdpDE is upregulated by the Agr/RNAIII system, which suggests that KdpDE may be an important virulence regulator coordinating the external K+sensing and Agr signaling during pathogenesis in this bacterium.
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20

Damnjanovic, Bojana, and Hans-Jürgen Apell. "Role of Protons in the Pump Cycle of KdpFABC Investigated by Time-Resolved Kinetic Experiments." Biochemistry 53, no. 19 (2014): 3218–28. http://dx.doi.org/10.1021/bi500336w.

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21

Greie, Jörg-Christian, and Karlheinz Altendorf. "The K+-translocating KdpFABC complex from Escherichia coli: A P-type ATPase with unique features." Journal of Bioenergetics and Biomembranes 39, no. 5-6 (2007): 397–402. http://dx.doi.org/10.1007/s10863-007-9111-0.

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22

Heitkamp, Thomas, René Kalinowski, Bettina Böttcher, Michael Börsch, Karlheinz Altendorf, and Jörg-Christian Greie. "K+-Translocating KdpFABC P-Type ATPase from Escherichia coli Acts as a Functional and Structural Dimer†." Biochemistry 47, no. 11 (2008): 3564–75. http://dx.doi.org/10.1021/bi702038e.

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23

Greie, Jörg-Christian. "The KdpFABC complex from Escherichia coli: A chimeric K+ transporter merging ion pumps with ion channels." European Journal of Cell Biology 90, no. 9 (2011): 705–10. http://dx.doi.org/10.1016/j.ejcb.2011.04.011.

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24

Heitkamp, Thomas, Bettina Böttcher, and Jörg-Christian Greie. "Solution structure of the KdpFABC P-type ATPase from Escherichia coli by electron microscopic single particle analysis☆." Journal of Structural Biology 166, no. 3 (2009): 295–302. http://dx.doi.org/10.1016/j.jsb.2009.02.016.

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25

Hu, Guo-Bin, William J. Rice, Stefan Dröse, Karlheinz Altendorf, and David L. Stokes. "Three-dimensional structure of the KdpFABC complex of Escherichia coli by electron tomography of two-dimensional crystals." Journal of Structural Biology 161, no. 3 (2008): 411–18. http://dx.doi.org/10.1016/j.jsb.2007.09.006.

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26

Schniederberend, Maren, Petra Zimmann, Mikhail Bogdanov, William Dowhan, and Karlheinz Altendorf. "Influence of K+-dependent membrane lipid composition on the expression of the kdpFABC operon in Escherichia coli." Biochimica et Biophysica Acta (BBA) - Biomembranes 1798, no. 1 (2010): 32–39. http://dx.doi.org/10.1016/j.bbamem.2009.10.002.

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27

Haupt, Melina, Marc Bramkamp, Markus Heller, et al. "The Holo-form of the Nucleotide Binding Domain of the KdpFABC Complex fromEscherichia coliReveals a New Binding Mode." Journal of Biological Chemistry 281, no. 14 (2005): 9641–49. http://dx.doi.org/10.1074/jbc.m508290200.

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28

Altendorf, K., P. Voelkner, and W. Puppe. "The sensor kinase KdpD and the response regulator KdpE control expression of the kdpFABC operon in Escherichia coli." Research in Microbiology 145, no. 5-6 (1994): 374–81. http://dx.doi.org/10.1016/0923-2508(94)90084-1.

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29

Rothenbücher, Marina C., Sandra J. Facey, Dorothee Kiefer, Marina Kossmann, and Andreas Kuhn. "The Cytoplasmic C-Terminal Domain of the Escherichia coli KdpD Protein Functions as a K+ Sensor." Journal of Bacteriology 188, no. 5 (2006): 1950–58. http://dx.doi.org/10.1128/jb.188.5.1950-1958.2006.

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ABSTRACT The KdpD protein is a K+ sensor kinase located in the cytoplasmic membrane of Escherichia coli. It contains four transmembrane stretches and two short periplasmic loops of 4 and 10 amino acid residues, respectively. To determine which part of KdpD functions as a K+ sensor, genetic variants were constructed with truncations or altered arrangements of the transmembrane segments. All KdpD constructs were tested by complementation of an E. coli kdpD deletion strain for their ability to grow at a K+ concentration of 0.1 mM in the medium. A soluble protein composed of the C-terminal cytoplasmic domain was able to complement the kdpD deletion strain. In addition, analysis of the β-galactosidase activity of an E. coli strain which carries a transcriptional fusion of the upstream region of the kdpFABC operon and a promoterless lacZ gene revealed that this soluble KdpD mutant responds to changes in the K+ concentration in the extracellular medium. The results suggest that the sensing and response functions are both located in the C-terminal domain and might be modulated by the N-terminal domain as well as by membrane anchoring.
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30

Ahnert, Franziska, Roland Schmid, Karlheinz Altendorf, and Jörg-Christian Greie. "ATP Binding Properties of the Soluble Part of the KdpC Subunit from theEscherichia coliK+-Transporting KdpFABC P-Type ATPase†." Biochemistry 45, no. 36 (2006): 11038–46. http://dx.doi.org/10.1021/bi061213p.

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31

Bramkamp, Marc, Karlheinz Altendorf, and Jörg-Christian Greie. "Common patterns and unique features of P-type ATPases: a comparative view on the KdpFABC complex fromEscherichia coli(Review)." Molecular Membrane Biology 24, no. 5-6 (2007): 375–86. http://dx.doi.org/10.1080/09687680701418931.

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32

Malli, Ravi, and Wolfgang Epstein. "Expression of the Kdp ATPase Is Consistent with Regulation by Turgor Pressure." Journal of Bacteriology 180, no. 19 (1998): 5102–8. http://dx.doi.org/10.1128/jb.180.19.5102-5108.1998.

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ABSTRACT The kdpFABC operon of Escherichia coliencodes the four protein subunits of the Kdp K+ transport system. Kdp is expressed when growth is limited by the availability of K+. Expression of Kdp is dependent on the products of the adjacent kdpDE operon, which encodes a pair of two-component regulators. Studies with kdp-lac fusions led to the suggestion that change in turgor pressure acts as the signal to express Kdp (L. A. Laimins, D. B. Rhoads, and W. Epstein, Proc. Natl. Acad. Sci. USA 78:464–468, 1981). More recently, effects of compatible solutes, among others, have been interpreted as inconsistent with the turgor model (H. Asha and J. Gowrishankar, J. Bacteriol. 175:4528–4537, 1993). We re-examined the effects of compatible solutes and of medium pH on expression of Kdp in studies in which growth rate was also measured. In all cases, Kdp expression correlated with the K+ concentration when growth began to slow. Making the reasonable but currently untestable assumptions that the reduction in growth rate by K+ limitation is due to a reduction in turgor and that addition of betaine does not increase turgor, we concluded that all of the data on Kdp expression are consistent with control by turgor pressure.
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33

Schrader, Michael, Klaus Fendler, Ernst Bamberg, et al. "Replacement of Glycine 232 by Aspartic Acid in the KdpA Subunit Broadens the Ion Specificity of the K+-Translocating KdpFABC Complex." Biophysical Journal 79, no. 2 (2000): 802–13. http://dx.doi.org/10.1016/s0006-3495(00)76337-5.

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34

Dubey, Vikas, David L. Stokes, Bjørn Panyella Pedersen, and Himanshu Khandelia. "An Intracellular Pathway Controlled by the N-terminus of the Pump Subunit Inhibits the Bacterial KdpFABC Ion Pump in High K+ Conditions." Journal of Molecular Biology 433, no. 15 (2021): 167008. http://dx.doi.org/10.1016/j.jmb.2021.167008.

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35

Bramkamp, Marc, and Karlheinz Altendorf. "Single Amino Acid Substitution in the Putative Transmembrane Helix V in KdpB of the KdpFABC Complex ofEscherichia coliUncouples ATPase Activity and Ion Transport†." Biochemistry 44, no. 23 (2005): 8260–66. http://dx.doi.org/10.1021/bi050135n.

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36

Haupt, Melina, Marc Bramkamp, Murray Coles, Karlheinz Altendorf, and Horst Kessler. "Inter-domain Motions of the N-domain of the KdpFABC Complex, a P-type ATPase, are not Driven by ATP-induced Conformational Changes." Journal of Molecular Biology 342, no. 5 (2004): 1547–58. http://dx.doi.org/10.1016/j.jmb.2004.07.060.

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37

Strahl, Henrik, and Jörg-Christian Greie. "The extremely halophilic archaeon Halobacterium salinarum R1 responds to potassium limitation by expression of the K+-transporting KdpFABC P-type ATPase and by a decrease in intracellular K+." Extremophiles 12, no. 6 (2008): 741–52. http://dx.doi.org/10.1007/s00792-008-0177-3.

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38

Siarot, Lowela, Hiroki Toyazaki, Makoto Hidaka, et al. "A Novel Regulatory Pathway for K+ Uptake in the Legume Symbiont Azorhizobium caulinodans in Which TrkJ Represses the kdpFABC Operon at High Extracellular K+ Concentrations." Applied and Environmental Microbiology 83, no. 19 (2017). http://dx.doi.org/10.1128/aem.01197-17.

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ABSTRACT Bacteria have multiple K+ uptake systems. Escherichia coli, for example, has three types of K+ uptake systems, which include the low-K+-inducible KdpFABC system and two constitutive systems, Trk (TrkAG and TrkAH) and Kup. Azorhizobium caulinodans ORS571, a rhizobium that forms nitrogen-fixing nodules on the stems and roots of Sesbania rostrata, also has three types of K+ uptake systems. Through phylogenetic analysis, we found that A. caulinodans has two genes homologous to trkG and trkH, designated trkI and trkJ. We also found that trkI is adjacent to trkA in the genome and these two genes are transcribed as an operon; however, trkJ is present at a distinct locus. Our results demonstrated that trkAI, trkJ, and kup were expressed in the wild-type stem nodules, whereas kdpFABC was not. Interestingly, Δkup and Δkup ΔkdpA mutants formed Fix– nodules, while the Δkup ΔtrkA ΔtrkI ΔtrkJ mutant formed Fix+ nodules, suggesting that with the additional deletion of Trk system genes in the Δkup mutant, Fix+ nodule phenotypes were recovered. kdpFABC of the Δkup ΔtrkJ mutant was expressed in stem nodules, but not in the free-living state, under high-K+ conditions. However, kdpFABC of the Δkup ΔtrkA ΔtrkI ΔtrkJ mutant was highly expressed even under high-K+ conditions. The cytoplasmic K+ levels in the Δkup ΔtrkA ΔtrkI mutant, which did not express kdpFABC under high-K+ conditions, were markedly lower than those in the Δkup ΔtrkA ΔtrkI ΔtrkJ mutant. Taking all these results into consideration, we propose that TrkJ is involved in the repression of kdpFABC in response to high external K+ concentrations and that the TrkAI system is unable to function in stem nodules. IMPORTANCE K+ is a major cytoplasmic cation in prokaryotic and eukaryotic cells. Bacteria have multiple K+ uptake systems to control the cytoplasmic K+ levels. In many bacteria, the K+ uptake system KdpFABC is expressed under low-K+ conditions. For years, many researchers have argued over how bacteria sense K+ concentrations. Although KdpD of Escherichia coli is known to sense both cytoplasmic and extracellular K+ concentrations, the detailed mechanism of K+ sensing is still unclear. In this study, we propose that the transmembrane TrkJ protein of Azorhizobium caulinodans acts as a sensor for the extracellular K+ concentration and that high extracellular K+ concentrations repress the expression of KdpFABC via TrkJ.
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39

Sweet, Marie E., Xihui Zhang, Hediye Erdjument-Bromage, et al. "Serine phosphorylation regulates the P-type potassium pump KdpFABC." eLife 9 (September 21, 2020). http://dx.doi.org/10.7554/elife.55480.

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KdpFABC is an ATP-dependent K+ pump that ensures bacterial survival in K+-deficient environments. Whereas transcriptional activation of kdpFABC expression is well studied, a mechanism for down-regulation when K+ levels are restored has not been described. Here, we show that KdpFABC is inhibited when cells return to a K+-rich environment. The mechanism of inhibition involves phosphorylation of Ser162 on KdpB, which can be reversed in vitro by treatment with serine phosphatase. Mutating Ser162 to Alanine produces constitutive activity, whereas the phosphomimetic Ser162Asp mutation inactivates the pump. Analyses of the transport cycle show that serine phosphorylation abolishes the K+-dependence of ATP hydrolysis and blocks the catalytic cycle after formation of the aspartyl phosphate intermediate (E1~P). This regulatory mechanism is unique amongst P-type pumps and this study furthers our understanding of how bacteria control potassium homeostasis to maintain cell volume and osmotic potential.
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40

Cholo, Moloko C., Maborwa T. Matjokotja, Ayman G. Osman, and Ronald Anderson. "Role of the kdpDE Regulatory Operon of Mycobacterium tuberculosis in Modulating Bacterial Growth in vitro." Frontiers in Genetics 12 (July 29, 2021). http://dx.doi.org/10.3389/fgene.2021.698875.

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Bacteria use K+-uptake transporters differentially for adaptation in varying growth conditions. In Mycobacterium tuberculosis, two K+-uptake systems, the Trk comprising the CeoB and CeoC proteins and the Kdp consisting of the two-component system (TCS), KdpDE and KdpFABC, have been characterized, but their selective utilization during bacterial growth has not been completely explored. In the current study, the roles of the M. tuberculosis KdpDE regulatory system alone and in association with the Trk transporters in bacterial growth were investigated by evaluating the growth of M. tuberculosis KdpDE-deletion and KdpDE/Trk (KT)-double knockout mutant strains in planktonic culture under standard growth conditions. The KT-double knockout mutant strain was first constructed using homologous recombination procedures and was evaluated together with the KdpDE-deletion mutant and the wild-type (WT) strains with respect to their rates of growth, K+-uptake efficiencies, and K+-transporter gene expression during planktonic growth. During growth at optimal K+ concentrations and pH levels, selective deletion of the TCS KdpDE (KdpDE-deletion mutant) led to attenuation of bacterial growth and an increase in bacterial K+-uptake efficiency, as well as dysregulated expression of the kdpFABC and trk genes. Deletion of both the KdpDE and the Trk systems (KT-double knockout) also led to severely attenuated bacterial growth, as well as an increase in bacterial K+-uptake efficiency. These results demonstrate that the KdpDE regulatory system plays a key role during bacterial growth by regulating K+ uptake via modulation of the expression and activities of both the KdpFABC and Trk systems and is important for bacterial growth possibly by preventing cytoplasmic K+ overload.
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41

Silberberg, Jakob M., Robin A. Corey, Lisa Hielkema, et al. "Deciphering ion transport and ATPase coupling in the intersubunit tunnel of KdpFABC." Nature Communications 12, no. 1 (2021). http://dx.doi.org/10.1038/s41467-021-25242-x.

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AbstractKdpFABC, a high-affinity K+ pump, combines the ion channel KdpA and the P-type ATPase KdpB to secure survival at K+ limitation. Here, we apply a combination of cryo-EM, biochemical assays, and MD simulations to illuminate the mechanisms underlying transport and the coupling to ATP hydrolysis. We show that ions are transported via an intersubunit tunnel through KdpA and KdpB. At the subunit interface, the tunnel is constricted by a phenylalanine, which, by polarized cation-π stacking, controls K+ entry into the canonical substrate binding site (CBS) of KdpB. Within the CBS, ATPase coupling is mediated by the charge distribution between an aspartate and a lysine. Interestingly, individual elements of the ion translocation mechanism of KdpFABC identified here are conserved among a wide variety of P-type ATPases from different families. This leads us to the hypothesis that KdpB might represent an early descendant of a common ancestor of cation pumps.
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42

Ali, Maria K., Xinfeng Li, Qing Tang, et al. "Regulation of Inducible Potassium Transporter KdpFABC by the KdpD/KdpE Two-Component System in Mycobacterium smegmatis." Frontiers in Microbiology 8 (April 24, 2017). http://dx.doi.org/10.3389/fmicb.2017.00570.

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43

Stock, C., L. Hielkema, I. Tascón, et al. "Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels." Nature Communications 9, no. 1 (2018). http://dx.doi.org/10.1038/s41467-018-07319-2.

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44

Wang, Xun, Xia Cai, Hongdan Ma, et al. "A c-di-AMP riboswitch controlling kdpFABC operon transcription regulates the potassium transporter system in Bacillus thuringiensis." Communications Biology 2, no. 1 (2019). http://dx.doi.org/10.1038/s42003-019-0414-6.

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45

Wang, Xun, Xia Cai, Hongdan Ma, et al. "Publisher Correction: A c-di-AMP riboswitch controlling kdpFABC operon transcription regulates the potassium transporter system in Bacillus thuringiensis." Communications Biology 2, no. 1 (2019). http://dx.doi.org/10.1038/s42003-019-0449-8.

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46

Haupt, Melina, Murray Coles, Horst Kessler, Marc Bramkamp, and Karlheinz Altendorf. "Inter-domain motions of the N-domain of the KdpFABC complex, a P-type ATPase, are not driven by ATP-induced conformational changes." GBM Annual Fall meeting M�nster 2004 2004, Fall (2004). http://dx.doi.org/10.1240/sav_gbm_2004_h_000763.

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47

Price-Whelan, Alexa, Chun Kit Poon, Meredith A. Benson, et al. "Transcriptional Profiling of Staphylococcus aureus During Growth in 2 M NaCl Leads to Clarification of Physiological Roles for Kdp and Ktr K+ Uptake Systems." mBio 4, no. 4 (2013). http://dx.doi.org/10.1128/mbio.00407-13.

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ABSTRACTStaphylococcus aureusexhibits an unusually high level of osmotolerance and Na+tolerance, properties that support survival in various host niches and in preserved foods. The genetic basis of these traits is not well understood. We compared the transcriptional profiles ofS. aureusgrown in complex medium with and without 2 M NaCl. The stimulon for growth in high-osmolality media and Na+included genes involved in uptake of K+, other compatible solutes, sialic acid, and sugars; capsule biosynthesis; and amino acid and central metabolism. Quantitative PCR analysis revealed that the loci responded differently from each other to high osmolality imposed by elevated NaCl versus sucrose. High-affinity K+uptake (kdp) genes and capsule biosynthesis (cap5) genes required the two-component system KdpDE for full induction by osmotic stress, withkdpAinduced more by NaCl andcap5Binduced more by sucrose. Focusing on K+importers, we identified threeS. aureus genes belonging to the lower-affinity Trk/Ktr family that encode two membrane proteins (KtrB and KtrD) and one accessory protein (KtrC). In the absence of osmotic stress, thektrgene transcripts were much more abundant than thekdpAtranscript. Disruption ofS. aureus kdpAcaused a growth defect under low-K+conditions, disruption ofktrCresulted in a significant defect in 2 M NaCl, and a ΔktrCΔkdpAdouble mutant exhibited both phenotypes. Protective effects ofS. aureusKtr transporters at elevated NaCl are consistent with previous indications that both Na+and osmolality challenges are mitigated by the maintenance of a high cytoplasmic K+concentration.IMPORTANCEThere is general agreement that the osmotolerance and Na+tolerance ofStaphylococcus aureusare unusually high for a nonhalophile and support its capacity for human colonization, pathogenesis, and growth in food. Nonetheless, the molecular basis for these properties is not well defined. The genome-wide response ofS. aureusto a high concentration, 2 M, of NaCl revealed the upregulation of expected genes, such as those for transporters of compatible solutes that are widely implicated in supporting osmotolerance. A high-affinity potassium uptake system, KdpFABC, was upregulated, although it generally plays a physiological role under very low K+conditions. At higher K+concentrations, a lower-affinity and more highly expressed type of K+transporter system, Ktr transporters, was shown to play a significant role in high Na+tolerance. This study illustrates the importance of the K+status of the cell for tolerance of Na+byS. aureusand underscores the importance of monovalent cation cycles in this pathogen.
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