ArticleProceedings of the National Academy of Sciences of the United States of America2010
Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 54 citations in OpenAlex.
- Identifying Functional Water Encapsulation Sites Within the Transmembrane Domain of Sensor Kinases.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The PhoPQ two-component regulatory system as an important regulator of bacterial stress response.Molecular biology reports · 2025Review
- Analysis of stress-induced small proteins inScience signaling · 2025Article
- Analysis of stress-induced small proteins inbioRxiv : the preprint server for biology · 2025Article
- An updated overview on the bacterial PhoP/PhoQ two-component signal transduction system.Frontiers in cellular and infection microbiology · 2025Review
- Atomic insights into the signaling landscape of E. coli PhoQ histidine kinase from molecular dynamics simulations.Scientific reports · 2024Article
- Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code.Nature communications · 2024Article
- Lipid A Modification and Metabolic Adaptation in Polymyxin-Resistant, New Delhi Metallo-β-Lactamase-Producing Klebsiella pneumoniae.Microbiology spectrum · 2023Article
- Membrane Sensor Histidine Kinases: Insights from Structural, Ligand and Inhibitor Studies of Full-Length Proteins and Signalling Domains for Antibiotic Discovery.Molecules (Basel, Switzerland) · 2021Review
- The ChvG-ChvI and NtrY-NtrX Two-Component Systems Coordinately Regulate Growth of Caulobacter crescentus.Journal of bacteriology · 2021Article
- Article
- Nitrate- and Nitrite-Sensing Histidine Kinases: Function, Structure, and Natural Diversity.International journal of molecular sciences · 2021Review
- Colistin Resistance Among Multiple Sequence Types ofFrontiers in microbiology · 2021Article
- Functional determinants of a small protein controlling a broadly conserved bacterial sensor kinase.Journal of bacteriology · 2020Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Actionable Activating Oncogenic ERBB2/HER2 Transmembrane and Juxtamembrane Domain Mutations.Cancer cell · 2018Article
- Structural insights into the signalling mechanisms of two-component systems.Nature reviews. Microbiology · 2018Review
- Osmosensing by the bacterial PhoQ/PhoP two-component system.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex.Scientific reports · 2017Article
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
PhoQ is the transmembrane sensor histidine kinase of the bacterial phoPQ two-component system, which detects and responds to divalent cations and to antimicrobial peptides, and can trigger virulence. Despite their ubiquitous importance in bacterial signaling, the structure and mechanism of the sensor kinases are not fully understood. In particular, the mechanism by which the signal is propagated through the transmembrane (TM) region remains unclear. We have identified a critical asparagine residue in the second TM helix of PhoQ. Replacement of this Asn202 with a variety of hydrophobic amino acids results in a protein that is blind to signal, fails to activate transcription of PhoQ-dependent genes, and abrogates transcription when coexpressed with wild-type PhoQ. Analysis of other two-component kinase sequences indicated that many such proteins contain similarly conserved polar residues, and the structure of one such domain shows a polar residue proximal to an extended cavity near the center of the TM bundle. We therefore examined the role of Asn202 in PhoQ. Our analysis indicated that its kinase function is dependent on the polarity of Asn202, rather than its precise structure or position in the TM region; it can be displaced up or down one turn of TM helix 2, or even moved to the adjacent TM helix 1. The presence of polar TM amino acids among many diverse sensor kinases suggest a widespread mechanism of two-component signal transduction; we speculate that they might stabilize underpacked water-containing cavities that can accommodate conformational changes required for switching from phosphatase to kinase-competent conformations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.