ArticleOpen biology2014
Mutational analysis of dimeric linkers in peri- and cytoplasmic domains of histidine kinase DctB reveals their functional roles in signal transduction.
Article in Open biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc.Nature communications · 2025Article
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- MifS, a DctB family histidine kinase, is a specific regulator of α-ketoglutarate response inMicrobiology (Reading, England) · 2020Article
- Structural and ligand binding analyses of the periplasmic sensor domain of RsbU in Chlamydia trachomatis support a role in TCA cycle regulation.Molecular microbiology · 2020Article
- State-of-the-art: functional fluorescent probes for bioimaging and pharmacological research.Acta pharmacologica Sinica · 2019Review
- Structural insights into the signalling mechanisms of two-component systems.Nature reviews. Microbiology · 2018Review
- Structural and Functional Analysis of the Escherichia coli Acid-Sensing Histidine Kinase EvgS.Journal of bacteriology · 2017Article
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Authors and funding
7 authors.
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Abstract
Membrane-associated histidine kinases (HKs) in two-component systems respond to environmental stimuli by autophosphorylation and phospho-transfer. HK typically contains a periplasmic sensor domain that regulates the cytoplasmic kinase domain through a conserved cytoplasmic linker. How signal is transduced from the ligand-binding site across the membrane barrier remains unclear. Here, we analyse two linker regions of a typical HK, DctB. One region connects the first transmembrane helix with the periplasmic Per-ARNT-Sim domains, while the other one connects the second transmembrane helix with the cytoplasmic kinase domains. We identify a leucine residue in the first linker region to be essential for the signal transduction and for maintaining the delicate balance of the dimeric interface, which is key to its activities. We also show that the other linker, belonging to the S-helix coiled-coil family, plays essential roles in signal transduction inside the cell. Furthermore, by combining mutations with opposing activities in the two regions, we show that these two signalling transduction elements are integrated to produce a combined effect on the final activity of DctB.
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