ArticleThe Journal of biological chemistry2019
Hydrogen exchange of chemoreceptors in functional complexes suggests protein stabilization mediates long-range allosteric coupling.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Signaling mechanism of the transmembrane energy receptor Aer.bioRxiv : the preprint server for biology · 2026Article
- Bacterial Chemoreceptors Transmit Stimulus Signals Through Coupled Entropic Switches.Journal of molecular biology · 2026Article
- Protein-protein interfaces in chemotaxis receptor complexes and their role in signaling.FEMS microbiology reviews · 2026Review
- Selective detection of a key region in chemotaxis signaling protein complexes by solid-state NMR.Biophysical journal · 2025Article
- Review
- Flavoproteins as native and genetically encoded spin probes for in cell ESR spectroscopy.Nature communications · 2025Article
- The structural logic of dynamic signaling in the Escherichia coli serine chemoreceptor.Protein science : a publication of the Protein Society · 2024Article
- The Structural Logic of Dynamic Signaling in thebioRxiv : the preprint server for biology · 2024Article
- Signal integration in chemoreceptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Attractant and repellent induce opposing changes in the four-helix bundle ligand-binding domain of a bacterial chemoreceptor.PLoS biology · 2023Article
- Bacterial chemoreceptor signaling complexes control kinase activity by stabilizing the catalytic domain of CheA.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Diethylpyrocarbonate-Based Covalent Labeling Mass Spectrometry of Protein Interactions in a Membrane Complex System.Journal of the American Society for Mass Spectrometry · 2023Article
- Structural signatures ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Characterization of Opposing Responses to Phenol by Bacillus subtilis Chemoreceptors.Journal of bacteriology · 2022Article
- Protein rings are critical to the remarkable signaling properties of bacterial chemotaxis nanoarrays.Science signaling · 2022Article
- Concerted Differential Changes of Helical Dynamics and Packing upon Ligand Occupancy in a Bacterial Chemoreceptor.ACS chemical biology · 2021Article
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
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3 authors at 1 institution in 1 country.
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Abstract
Bacterial chemotaxis receptors form extended hexagonal arrays that integrate and amplify signals to control swimming behavior. Transmembrane signaling begins with a 2-Å ligand-induced displacement of an α helix in the periplasmic and transmembrane domains, but it is unknown how the cytoplasmic domain propagates the signal an additional 200 Å to control the kinase CheA bound to the membrane-distal tip of the receptor. The receptor cytoplasmic domain has previously been shown to be highly dynamic as both a cytoplasmic fragment (CF) and within the intact chemoreceptor; modulation of its dynamics is thought to play a key role in signal propagation. This hydrogen deuterium exchange-MS (HDX-MS) study of functional complexes of CF, CheA, and CheW bound to vesicles in native-like arrays reveals that the CF is well-ordered only in its protein interaction region where it binds CheA and CheW. We observe rapid exchange throughout the rest of the CF, with both uncorrelated (EX2) and correlated (EX1) exchange patterns, suggesting the receptor cytoplasmic domain retains disorder even within functional complexes. HDX rates are increased by inputs that favor the kinase-off state. We propose that chemoreceptors achieve long-range allosteric control of the kinase through a coupled equilibrium: CheA binding in a kinase-on conformation stabilizes the cytoplasmic domain, and signaling inputs that destabilize this domain (ligand binding and demethylation) disfavor CheA binding such that it loses key contacts and reverts to a kinase-off state. This study reveals the mechanistic role of an intrinsically disordered region of a transmembrane receptor in long-range allostery.
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