ArticleJournal of molecular biology2016
Bacterial Chemoreceptor Dynamics: Helical Stability in the Cytoplasmic Domain Varies with Functional Segment and Adaptational Modification.
Article in Journal of molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- 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
- A chemoreceptor conformational equilibrium controlled by signaling inputs.Proceedings of the National Academy of Sciences of the United States of America · 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
- A nonequilibrium allosteric model for receptor-kinase complexes: The role of energy dissipation in chemotaxis signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural signatures ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Characterization of Opposing Responses to Phenol by Bacillus subtilis Chemoreceptors.Journal of bacteriology · 2022Article
- Allostery and protein plasticity: the keystones for bacterial signaling and regulation.Biophysical reviews · 2021Review
- Concerted Differential Changes of Helical Dynamics and Packing upon Ligand Occupancy in a Bacterial Chemoreceptor.ACS chemical biology · 2021Article
- Studying bacterial chemosensory array with CryoEM.Biochemical Society transactions · 2021Review
- Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.Biochimica et biophysica acta. Biomembranes · 2020Article
- Regulation of the chemotaxis histidine kinase CheA: A structural perspective.Biochimica et biophysica acta. Biomembranes · 2020Review
- Hydrogen exchange of chemoreceptors in functional complexes suggests protein stabilization mediates long-range allosteric coupling.The Journal of biological chemistry · 2019Article
- Carbon-nitrogen REDOR to identify ms-timescale mobility in proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Article
- Conformational shifts in a chemoreceptor helical hairpin control kinase signaling inProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Inverted signaling by bacterial chemotaxis receptors.Nature communications · 2018Article
- A dual regulation mechanism of histidine kinase CheA identified by combining network-dynamics modeling and system-level input-output data.PLoS computational biology · 2018Article
- A zipped-helix cap potentiates HAMP domain control of chemoreceptor signaling.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.The journal of physical chemistry. B · 2017Article
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2 authors at 1 institution in 1 country.
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Abstract
Dynamics are thought to be important features of structure and signaling in the cytoplasmic domain of bacterial chemoreceptors. However, little is known about which structural features are dynamic. For this largely helical domain, comprising a four-helix bundle and an extended four-helix coiled coil, functionally important structural dynamics likely involves helical mobility and stability. To investigate, we used continuous wave EPR spectroscopy and site-specific spin labels that directly probed, in essentially physiological conditions, the mobility of helical backbones in the cytoplasmic domain of intact chemoreceptor Tar homodimers inserted into lipid bilayers of Nanodiscs. We observed differences among functional regions, between companion helices in helical hairpins of the coiled coil and between receptor conformational states generated by adaptational modification. Increased adaptational modification decreased helical dynamics while preserving dynamics differences among functional regions and between companion helices. In contrast, receptor ligand occupancy did not have a discernable effect on dynamics to which our approach was sensitive, implying that the two sensory inputs alter different chemoreceptor features. Spectral fitting indicated that differences in helical dynamics we observed for ensemble spin-label mobility reflected differences in proportions of a minority receptor population in which the otherwise helical backbone was essentially disordered. We suggest that our measurements provided site-specific snapshots of equilibria between a majority state of well-ordered helix and a minority state of locally disordered polypeptide backbone. Thus, the proportion of polypeptide chain that is locally and presumably transiently disordered is a structural feature of cytoplasmic domain dynamics that varies with functional region and modification-induced signaling state.
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