Stimulus Perception and Signal Transduction by Histidine Kinases
Two-component systems, which are predominantly found in bacteria and archaea, are based on phosphotransfer from a histidine protein kinase to a response regulator. Signaling starts with a stimulus-dependent autophosphorylation of the histidine kinase. The phosphoryl group is then transferred to an aspartate residue in the receiver domain of the response regulator. The latter event induces conformational alterations in the response regulator, thereby affecting nucleic acid binding, enzymatic activity, or protein interactions of the effector domain. We found that the K+ responsive histidine kinase KdpD in E. coli employs two accessory components, the universal stress protein UspC and the phosphotransferase system component IIANtr, that interact with the kinase to fine-tune kdpFABC expression according to the cellular requirements. Current research focuses on the structural characterization of histidine kinase KdpD. In addition, the nature of the stimulus as well as the target genes of the thus far non-characterized histidine protein kinase YehU and the cognate response regulator YehT of E. coli are analyzed by combined transcriptome and proteome approaches.
Schemes of the diverse phospho-regulation mechanisms of protein kinases. (A) Stimulus perception and signaling by a histidine protein kinase/response regulator system (B) Signaling by protein kinases that target serine, threonine, or tyrosin residues is illustrated by a MAPK pathway. (C) Heat stress induces the activity of the arginine protein kinase McsB of B. subtilis , which phosphorylates the transcriptional regulator CtsR.
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Jung, K., Fried, L., Behr, S., Heermann, R. (2012) Histidine Kinases and Response Regulators in Networks, Curr. Opin. Microbiol. Apr;15(2):118-24.
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Heermann, R., Weber, A., Mayer, B., Ott, M., Hauser, E., Gabriel, G., Pirch, T., Jung, K. (2009) The universal stress protein UspC scaffolds the KdpD/KdpE signaling cascade of Escherichia coli under salt stress, J. Mol. Biol., 386, 134-148.
Lüttmann, D., Heermann, R., Zimmer, B., Hillmann, A., Rampp I.S., Jung, K., Görke, B. (2009) Stimulation of the potassium sensor KdpD kinase activity by interaction with the phosphotransferase protein IIANtr in Escherichia coli. Mol. Microbiol., 72, 978-994.
Heermann, R., Lippert, M.-L., Jung, K. (2009) Domain swapping reveals that the N-terminal domain of the sensor kinase KdpD in Escherichia coli is important for signaling, BMC Microbiology, 9,133.
Fleischer, R., Heermann, R., Jung, K., Hunke, S. (2007) Purification, reconstitution and characterization of the CpxRAP envelope stress system of Escherichia coli, J. Biol. Chem., 282, 8583-8593.
Zimmann, P., Steinbrügge, A., Schniederberend, M., Jung, K., Altendorf, K. (2007) The extension of the fourth transmembrane helix of the sensor kinase KdpD of Escherichia coli is involved in sensing, J. Bacteriol. 189, 7326-7334.
Heermann, R., Altendorf, K., Jung, K. (2003) The N-terminal input domain of the sensor kinase KdpD of Escherichia coli stabilizes the interaction between the cognate response regulator KdpE and the corresponding DNA-binding site, J. Biol. Chem. 278(51):51277-84.
Heermann, R., Fohrmann, A., Altendorf, K., Jung, K. (2003) The transmembrane domains of the sensor kinase KdpD of Escherichia coli are not essential for sensing K+ limitation, Mol. Microbiol. 47(3):839-848.
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