ArticleProceedings of the National Academy of Sciences of the United States of America2017
Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Mechanism of sensor kinase CitA transmembrane signaling.Nature communications · 2025Article
- Development of Malate Biosensor-Containing Hydrogels and Living Cell-Based Sensors.International journal of molecular sciences · 2024Article
- Article
- Article
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- 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
- Conversion of the Sensor Kinase DcuS to the Fumarate Sensitive State by Interaction of the Bifunctional Transporter DctA at the TM2/PASMicroorganisms · 2021Article
- Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning.Biomolecules · 2021Article
- Interface switch mediates signal transmission in a two-component system.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- High-Performance Intensiometric Direct- and Inverse-Response Genetically Encoded Biosensors for Citrate.ACS central science · 2020Article
- Structural insights into the signalling mechanisms of two-component systems.Nature reviews. Microbiology · 2018Review
- Transmembrane signaling and cytoplasmic signal conversion by dimeric transmembrane helix 2 and a linker domain of the DcuS sensor kinase.The Journal of biological chemistryArticle
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8 authors.
Funding
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Abstract
Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of the PAS domain, which is well characterized for the isolated domain, is the signal transmitted to the transmembrane (TM) helices in a CitA construct in liposomes. Putting the extracytoplasmic PAS domain into context of the membrane-embedded CitA construct slows down citrate-binding kinetics by at least a factor of 60, confirming that TM helix motions are linked to the citrate-binding event. Our results are confirmation of a hallmark of the HK signal transduction mechanism with atomic resolution on a full-length construct lacking only the kinase core domain.
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