A structure-function study of ZraP and ZraS provides new insights into the two-component system Zra

Taher, Raleb; Rosny, Eve de

doi:10.1016/j.bbagen.2020.129810

Cited by 7 publications

(9 citation statements)

References 32 publications

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Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

“…A third characterized Zn-binding two-component system is the zinc resistance associated system, or ZraSR, which is known to be present in several pathogens including E. coli , S. enterica , and Proteus mirabilis . − Unlike the WalKR and BaeSR systems, the ZraSR system is unique, as it contains a third periplasmic repressor partner, ZraP, in addition to its sensor HK, ZraS, and its RR, ZraR . The ZraSR system is responsive to Zn 2+ concentrations; high Zn 2+ concentrations are sensed by the ZraSR system that then contributes to the activation of metal tolerance genes and, once stable, represses itself by activating the expression of zraP . The third protein of this system, ZraP, is an important Zn-binding soluble protein expressed under Zn 2+ stress conditions and has been reported to act as a Zn 2+ -dependent molecular chaperone. , The binding of Zn 2+ to ZraP causes an ATP-independent oligomeric change (from monomer to octamer) that significantly increases ZraP’s stability and function. , The structure of Zn 2+ -bound ZraP reveals the presence of four interfacial Zn 2+ -binding sites that contribute to its oligomeric stability .…”

Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

“…The ZraSR system is responsive to Zn 2+ concentrations; high Zn 2+ concentrations are sensed by the ZraSR system that then contributes to the activation of metal tolerance genes and, once stable, represses itself by activating the expression of zraP . The third protein of this system, ZraP, is an important Zn-binding soluble protein expressed under Zn 2+ stress conditions and has been reported to act as a Zn 2+ -dependent molecular chaperone. , The binding of Zn 2+ to ZraP causes an ATP-independent oligomeric change (from monomer to octamer) that significantly increases ZraP’s stability and function. , The structure of Zn 2+ -bound ZraP reveals the presence of four interfacial Zn 2+ -binding sites that contribute to its oligomeric stability . It has been proposed that this two-component system participates in cellular Zn 2+ balance as well as Zn 2+ overload protection via metal ion sequestration via ZraP .…”

Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

“…The third protein of this system, ZraP, is an important Zn-binding soluble protein expressed under Zn 2+ stress conditions and has been reported to act as a Zn 2+ -dependent molecular chaperone. , The binding of Zn 2+ to ZraP causes an ATP-independent oligomeric change (from monomer to octamer) that significantly increases ZraP’s stability and function. , The structure of Zn 2+ -bound ZraP reveals the presence of four interfacial Zn 2+ -binding sites that contribute to its oligomeric stability . It has been proposed that this two-component system participates in cellular Zn 2+ balance as well as Zn 2+ overload protection via metal ion sequestration via ZraP . In addition to sensing Zn 2+ , experiments have also found that ZraSR regulates hydrogenase 3 formation, a portion of the formate hydrogen lyase complex that is involved in fermentative H 2 production, which is a significant product in microbial metabolism .…”

Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

“…196,197 The binding of Zn 2+ to ZraP causes an ATPindependent oligomeric change (from monomer to octamer) that significantly increases ZraP's stability and function. 45,196 The structure of Zn 2+ -bound ZraP reveals the presence of four interfacial Zn 2+ -binding sites that contribute to its oligomeric stability. 198 It has been proposed that this two-component system participates in cellular Zn 2+ balance as well as Zn 2+ overload protection via metal ion sequestration via ZraP.…”

Section: ■ Copper Sensing Two-component Systemsmentioning

confidence: 99%

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Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems

Paredes,

Iheacho,

Smith

2023

Biochemistry

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Bacteria survive in highly dynamic and complex environments due, in part, to the presence of systems that allow the rapid control of gene expression in the presence of changing environmental stimuli. The crosstalk between intra-and extracellular bacterial environments is often facilitated by two-component signal transduction systems that are typically composed of a transmembrane histidine kinase and a cytosolic response regulator. Sensor histidine kinases and response regulators work in tandem with their modular domains containing highly conserved structural features to control a diverse array of genes that respond to changing environments. Bacterial two-component systems are widespread and play crucial roles in many important processes, such as motility, virulence, chemotaxis, and even transition metal homeostasis. Transition metals are essential for normal prokaryotic physiological processes, and the presence of these metal ions may also influence pathogenic virulence if their levels are appropriately controlled. To do so, bacteria use transition-metal-sensing two-component systems that bind and respond to rapid fluctuations in extracytosolic concentrations of transition metals. This perspective summarizes the structural and metal-binding features of bacterial transition-metal-sensing two-component systems and places a special emphasis on understanding how these systems are used by pathogens to establish infection in host cells and how these systems may be targeted for future therapeutic developments.

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Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

Section: Zinc Sensing Two-component Systemsmentioning

confidence: 99%

Section: ■ Copper Sensing Two-component Systemsmentioning

confidence: 99%

See 3 more Smart Citations

Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems

Paredes,

Iheacho,

Smith

2023

Biochemistry

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Dissection of the antibacterial mechanism of zinc oxide nanoparticles with manipulable nanoscale morphologies

Zhu

Wang

Cai

et al. 2022

Journal of Hazardous Materials

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Response to substrate limitation by a marine sulfate-reducing bacterium

et al. 2021

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Sulfate-reducing microorganisms (SRM) in subsurface sediments live under constant substrate and energy limitation, yet little is known about how they adapt to this mode of life. We combined controlled chemostat cultivation and transcriptomics to examine how the marine sulfate reducer, Desulfobacterium autotrophicum, copes with substrate (sulfate or lactate) limitation. The half-saturation uptake constant (Km) for lactate was 1.2 µM, which is the first value reported for a marine SRM, while the Km for sulfate was 3 µM. The measured residual lactate concentration in our experiments matched values observed in situ in marine sediments, supporting a key role of SRM in the control of lactate concentrations. Lactate limitation resulted in complete lactate oxidation via the Wood–Ljungdahl pathway and differential overexpression of genes involved in uptake and metabolism of amino acids as an alternative carbon source. D. autotrophicum switched to incomplete lactate oxidation, rerouting carbon metabolism in response to sulfate limitation. The estimated free energy was significantly lower during sulfate limitation (−28 to −33 kJ mol−1 sulfate), suggesting that the observed metabolic switch is under thermodynamic control. Furthermore, we detected the upregulation of putative sulfate transporters involved in either high or low affinity uptake in response to low or high sulfate concentration.

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A structure-function study of ZraP and ZraS provides new insights into the two-component system Zra

Cited by 7 publications

References 32 publications

Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems

Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems

Dissection of the antibacterial mechanism of zinc oxide nanoparticles with manipulable nanoscale morphologies

Response to substrate limitation by a marine sulfate-reducing bacterium

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